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Anatomy and Physiology 1 > Chapters 1-3 > Flashcards

Chapters 1-3 Flashcards

1
Q

Definition of Anatomy

A

The study of the internal and external structures of the body and the relationships between the body parts

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2
Q

Relationship between Anatomy and Physiology

A

All specific functions are performed by specific structures.

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3
Q

Areas of Anatomy

A

Gross Anatomy (macroscopic)

Surface Anatomy

Regional Anatomy

Systemic Anatomy

Developmental Anatomy (Conception to maturity)

  Embryology – first 2 months of development

Clinical – pathological, radiographic, surgical

Microscopic Anatomy

Cytology

Histology

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4
Q

Areas of Physiology

A

Cell Physiology
Organ Physiology
Systemic Physiology
Pathological Physiology

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5
Q

Definition of Physiology

A

The study of how living organisms perform their vital functions.

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6
Q

Definitions of Tissue, Organ and Organ System

A
  • *Tissue:** A group of cells working together to perform a function.
  • *Organ:** A group of tissues working together to perform a function.
  • *Organ System: ** A group of organs interacting to perform a function.
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7
Q

Integumentary System

Organs and Functions

A

Skin
Hair
Nails
Sweat Glands

  • Protect against environmental hazards
  • Helps regulate body temperature
  • Provides sensory information
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8
Q

Skeletal System

Organs and Functions

A

Bones

Cartilage

Associated Ligaments

Bone Marrow

  • Provides support and protection for other tissues
  • Stores calcium and other minerals
  • Forms blood cells
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9
Q

Muscular System

Organs and Function

A

Skeletal muscles

Associated Tendons

Cartilage

Bone Marrow

  • Provide protection and support for other tissues.
  • Generates heat that maintains body temperature
  • Provide movement
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10
Q

Nervous System

Organs and Functions

A

Brain
Spinal Chord
Peripheral Nerves
Sense Organs

  • Directs immediate responses to stimuli.
  • Coordinates or moderates activities of other organ systems.
  • Provides and interprets sensory information about external stimuli.
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11
Q

Endocrine System

Organs and Functions

A

Pituitary
Thyroid
Pancreas
Adrenal Gland
Gonads
Endocrine tissues in
other systems

  • Directs long term changes in the activities of other systems.
  • Adjusts metabolic activity and energy use by the body
  • Controls many structural and functional changes during development
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12
Q

Cardiovascular System

Organs and Functions

A

Heart

Blood

Blood Vessels

  • Distributes blood, cells, water and dissolved materials including blood, waste materials, nutrients, oxygen and CO2
  • Distributes heat and assists in regulating body temperature.
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13
Q

Lymphatic System

Organs and Functions

A

Spleen
Thymus
Lymphatic Vessels
Lymph Nodes
Tonsils

  • Defends against infection and disease
    • Returns tissue fluids to the blood stream
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14
Q

Respiratory System

Organs and Functions

A

Nasal Cavities
Sinuses
Larynx
Trachea
Lungs
Bronchi
Alvioli

  • Delivers air to alvioli
  • Provides oxygen to bloodstream
  • Removes CO2 from the bloodstream
  • Produces sounds for communication
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15
Q

Digestive System

Organs and Functions

A

Teeth
Tongue
Pharynx
Esophagus
Stomach
Large Intestine
Small Intestine
Liver
Gallbladder
Pancreas

  • Process and digests food
  • Absorbs and conserves water
  • Absorbs nutrients
  • Stores energy reserves
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16
Q

Urinary System

Organs and Functions

A

Kidneys
Ureters
Urinary bladder
Urethra

  • Excretes waste products from the blood
  • Controls water balance by regulating the volume of urine produced
  • Stores urine prior to voluntary elimination.
  • Regulates blood ion concentrations and PH
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17
Q

Male Reproductive System

Organs and Functions

A

Testes
Epididymides
Ductus Deferentia
Seminal Vesicles
Prostate Gland
Penis
Scrotum

  • Produces male sex cells (sperm), suspending fluids and hormones
  • Sexual intercourse
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18
Q

Female Reproductive System

Organs and Functions

A

Ovaries • Produces female sex cells and their hormones
Uterine Tubes • Supports developing embryo from conception to delivery
Uterus • Provides milk to nourish newborn infant.
Vagina • Sexual intercourse
Labia
Clitoris
Mamary Glands

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19
Q

What helps to maintain PH?

A

The kidneys regulate blood ion concentration and PH levels

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20
Q

Define Homeostatis and Homeostatic Regulation

A

Homeostasis: The existence of a stable internal environment.
Homeostatic Regulation: The adjustment of physiological systems to preserve homeostasis.
When the body fails to achieve homeostatic regulation, illness or disease sets in.

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21
Q

What are the two general mechanisms involved in Homeostasis?

A
  • *Auto Regulation**: When a cell, tissue, organ or organs system adjusts its activities automatically in response to some environmental change.
  • *Extrinsic Regulation:** When the nervous system or endocrine systems respond to stimuli to return to homeostasis.
  • The nervous system directs rapid, short-term, and very specific responses. Example: contraction of muscles to move hand away from a hot stove.
  • The endocrine system releases chemical messengers, hormones, which affect tissues and organs throughout the body. Examples: long-term regulation of blood volume and composition and the adjustment of organ system function during starvation.
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22
Q

Explain the three parts of homeostatic regulatory mechanism.

A
  • *Receptor**: A sensor that is sensitive to a particular stimulus or environmental change
  • *Control Center:** Receives, processes, and responds to the information supplied by the receptor.
  • *Effector**: A cell or organ that responds to the commands of the control center and whose activity either opposes or enhances the stimulus.
  • *Set point:** The desired value that achieves homeostasis.
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23
Q

Explain Negative Feedback

A
  • *Negative Feedback**: The primary mechanism of homeostatic regulation. It opposes or negates a variation from normal limits.
  • It maintains a normal range rather than a fixed value. The set point may vary with changing environments or differing activity levels.
  • The variability is greater among individuals than within an individual.
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24
Q

Defiene Dynamic Equilibrium

A

Dynamic Equilibrium: When the body continually adapts to maintain homeostatic regulation. Each physiological system functions to maintain a state of equilibrium that keeps vital conditions within normal limits.

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25
Q

Role of Organ Systems in Homeostatic Regulation for

Body Temperature.

A

Integumentary System: Heat loss
Muscular System: Heat production
Cardiovascular System: Heat distribution
Nervous System: Coordination of blood flow, heat production and heat loss.

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26
Q

Explain positive feedback

A

Positive Feedback: an initial stimulus produces a response that exaggerates or enhances the original change in conditions.
Positive feedback loops are typically found when a potentially dangerous or stressful process must be completed quickly before homeostasis can be restored.
Examples: Blood clotting (Hypovolemic shock - failure to clot) and childbirth (oxytocin).

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27
Q

Explain the role of insulin and glucagon in maintaining homeostasis

A

Insulin and glucagon are hormones secreted by islet cells within the pancreas. They are both secreted in response to blood sugar levels, but in opposite fashion!
Insulin is normally secreted by the beta cells (a type of islet cell) of the pancreas. The stimulus for insulin secretion is a HIGH blood glucose. The amount secreted into the blood increases as the blood glucose rises. As blood glucose falls, the amount of insulin secreted by the pancreatic islets goes down. In response to insulin, muscle cells, red blood cells and fat cells absorb glucose out of the blood, having the net effect of lowering the high blood glucose levels into the normal range.
Glucagon is secreted by the alpha cells of the pancreatic islets in much the same manner as insulin…except in the opposite direction. When blood glucose goes LOW, however, (such as between meals, and during exercise) more and more glucagon is secreted. The effect of glucagon is to make the liver release the glucose it has stored in its cells into the bloodstream, with the net effect of increasing blood glucose.
Our bodies desire blood glucose to be maintained between 70 mg/dl and 110 mg/dl (mg/dl means milligrams of glucose in 100 milliliters of blood). Below 70 is termed “hypoglycemia.” Above 110 can be normal if you have eaten within 2 to 3 hours. Above 180 is termed “hyperglycemia” (which translates to mean “too much glucose in the blood”). If your 2 two blood sugar measurements above 200 after drinking a sugar-water drink (glucose tolerance test),
then you are diagnosed with diabetes.

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28
Q

Definitions:

Electon Cloud

Electon Shell

Valence shell

A

Electron Cloud: The spherical area in which electrons travel

Electron Shell: a 2-dimensional representation of where the electrons circulate due to the electrical force created by the

 negative electrons and positive protons.

Valence shell: the outer energy level of the atom. The number of electrons in the level determines the chemical properties of the element.

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29
Q

Definitions:

Atoms

Atomic Number

Mass Number

Element

Isotope

A

Atoms: The smallest stable unit of matter
3 subatomic particles: Protons, Neutrons and Electrons
Atomic number: The amount of protons (and electrons)
Mass number: the total number of protons and neutrons
Element: all atoms with the same atomic number
Isotopes: Atoms of the same element whose nuclei have the same number of protons but a different number of neutrons.

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30
Q

Definitions:

Compound

Molecule

A
  • *Compound:** a chemical substance made up of atoms of two or more different chemical substances.
  • *Molecule:** a chemical structure consisting of two or more atoms held together by covalent bonds.
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31
Q

Definitions

Ion

Cation

Anion

A
  • *Ions:** Atoms or molecules that carry an electric charge
  • *Cations:** Ions with a positive charge
  • *Anions:** Ions with a negative charge
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32
Q

Ionic Bond

A

A chemical bond where an atom with an unfilled valence shell donates an electron to another atom so that both become stable ions. The electron donor becomes a cation (+ charge) and the electron acceptor becomes an anion (- charge). The electrical attraction between the newly formed cation and anion draw the two atoms together.

Example: Sodium and Chorine attach to form NaCl. Sodium donates an electron to Chlorine so sodium becomes Na+ and chlorine becomes Cl-.

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33
Q

Common Elements in the body and their functions:

Oxygen, Carbon, Hydrogen, Nitrogen

Calcium, Phosphorus, Potassium, Sodium

A
  • *Oxygen** – Component of water. Essential for respiration
  • *Carbon** - Found in all organic molecules
  • *Hydrogen** – component of water and most other molecules in body
  • *Nitroge**n – Found in proteins and nucleic acids. Form bases of DNA.
  • *Calcium** – Found in bones and teeth. Important for membrane function, nerve impulses, muscle contraction and blood clotting.
  • *Phosphoru**s – Found in bones and teeth, nucleic acids and high- energy compunds.
  • *Potassium** – Important for membrane function, nerve impulses, and muscle contraction.
  • *Sodium** – Import for blood volume, membrane function, nerve impulses and muscle contraction.
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34
Q

Covalent Bonds

A

Chemical bonds where electrons in the incomplete outer level are shared by the atoms.
Single covalent bond – one pair is shared. Hydrogen
Double covalent bond – two pairs are shared. Oxygen
Triple covalent bond – three electron pairs are shared. Nitrogen

  • *Polar covalent bonds** – electrons are not shared equally. H2O
  • *Nonpolar covalent bonds** – electrons are shared equally
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35
Q

Hydrogen Bond

A

A weak bond that acts between molecules or between atoms with a molecule. It is the bond between a partial positive charge of a hydrogen atom with a partial negative charge of an oxygen, nitrogen or fluorine atom of another covalent bond. It can change molecular shapes or pull molecules together.
Creates surface tension in water. Allows insects to walk on water and small particles of dust from touching the surface of the eye.

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36
Q

Chemical Reaction

A

New chemical bonds from between atoms or existing chemical bonds are broken.
Atoms in the reacting substances, reactants, are rearranged to form different substances or products.

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37
Q

Metabolism

A

All chemical reactions occurring in the body at any given moment.

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38
Q

Octet Rule

A

Atoms of low (<20) atomic number tend to combine in such a way that they each have eight electrons in their valence shell (other than the first shell which only carries 2 electrons.)

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39
Q

Energy

A

Energy: The capacity to perform work. Energy cannot be created or destroyed.
_Kinetic energy: _ Energy of motion.
Potential Energy: Stored energy.

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40
Q

Catabolism:

A

The decomposition reactions of complex molecules within the body’s cells and tissues.
When a covalent bond (a form of potential energy) is broken, it releases kinetic energy that can perform work. This way, cells perform vital functions such as growth, movement and reproduction.

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41
Q

Decomposition Reaction

A

Decomposition Reaction: a decomposition reaction involving water, breaking a molecule into smaller fragments. Occurs outside of cells as well as within them.
AB→ A+ B
Hydrolosis: One of the bonds of the molecule is broke and the components of a water molecule are added to the resulting fragments. (The water loosens the molecule and bonds to the components)
A-B+H2O→ A-H+HO-B

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42
Q

Synthesis Reaction

A

Synthesis Reaction: assembles smaller molecules into larger molecules and always involves the formation of new chemical bonds. An example is the formation of water from hydrogen and oxygen molecules.
A+B→AB
Dehydration Synthesis: Formation of a complex molecule by the removal of a water molecule.
A-H+HO-B→A-B+H20

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43
Q

Anabolism

A

Anabolism: The synthesis of new molecules within the body’s cells and tissues. Since it takes energy to create a chemical bond, anabolism is considered an “uphill” process.

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44
Q

Exchange Reaction

A

Parts of the reacting molecules are shuffled around to produce new products. Contains decomposition and synthesis.
AB+CK→AD+CB

45
Q

Reversible Reaction

A

Chemical reactions reversible. Decomposition and Synthesis occur simultaneously. (Jello)
A+B← and → AB

46
Q

Enzyme

A

A protein catalyst that lowers the activation energy of a reaction. Enzymic reactions are reversible. The enzyme only affects the rate of reaction.

47
Q

Metabolites and Nutrients

A
  • *Metabolites:** All the molecules (including nutrients) that can be synthesized or broken down by chemical reactions inside our bodies.
  • *Nutrients:** Essential elements and molecules normally obtained from the diet.
48
Q

Inorganic Compounds in our bodies

A

Water

Carbon Dioxide

Oxygen

Inorganic acids, bases and salts

49
Q

Properties of Water

A

Solubility
Reactivity – chemical reactions in our body occur in water and water is a participant in some reactions (hydrolosis and dehydration synthesis)
High Heat Capacity
Water stays in a liquid state for a long time. Keeps our blood from boiling or freezing.
Carries a lot of heat away with it when it changes to a gas. Responsible for cooling effect of perspiration.
Thermal inertia: water changes temperature slowly so it helps to stabilize body temp.
Lubrication

50
Q

Dissociation (Ionization)

A

Ionic bonds are broken as the individual ions interact with the positive or negative ends of polar water molecules. This results in a mixture of cations and anions surrounded by water molecules. The water molecules on each ion form a hydrogen sphere. (Example: NaCl)

51
Q

Electrolytes

A

Soluble inorganic compounds whose ions will conduct an electrical current in solution. Changes in the concentrations of electrolytes in body fluids disturb almost every vital function. The concentration of ions in body fluids are regulated by the kidneys (ion excretion), digestive tract (ion absorption) and skeletal system (ion storage).

52
Q

Amphipathic

A

Of, or relating to, a molecule having hydrophobic and hydrophilic regions.

53
Q

pH, acids, and bases

A

Power of hydrogen. The negative logarithm of the hydrogen concentration in moles per liter.
PH scale: 01-14. Proper pH of body fluids is necessary for body to maintain homeostasis.
Neutral: 7
Acid: <7 (hydrochloric acid, stomach acid, beer, vinegar, wine, pickles,tomatoes, grapes, saliva, milk). More hydrogen ions than hydroxide ions.
Base: >7 (Sodium hydroxide, Oven cleaner, household ammonia, household bleach, ocean water, eggs, blood) More hydroxide ions than hydrogen ions.
pH of blood – 7.35-7.45. Abnormal fluctuations in pH can damage cells and tissues by beaking chemical bonds, changing the shapes of proteins and altering cellular functins.
Acidosis: pH<7.35. pH<7 can produce a coma.
Alkalosis pH>7.45. pH>7.8 causes uncontrollable and sustained skeletal muscle contractions.

54
Q

Definition of Acid

A

Any solute that dissociates in solution and releases hydrogen ions, thereby lowering the pH. (proton donor)

55
Q

Definition of Base

A

A solute that removes hydrogen ions from a solution and thereby raises the pH. (proton acceptor)

56
Q

Definition of Salt

A

An ionic compound containing any cation except a hydrogen ion and any anion except a hydroxide ion. Salts dissociate freely in water, releasing cations and anions.

57
Q

4 Types of Organic Compounds

A

Carbohydrates

Lipids

Proteins

Nucleic Acids

58
Q

Definition of Buffer

A

Buffers: Compounds that stabilize the pH of a solution by removing or replacing hydrogen ions. They usually involve a weak acid and its related salt, which acts like a weak base.
• Sodium bicarbonate is very important in the human body.
• Baking soda will neutralize an overdose of aspirin.

Antacids: Basic compounds that neutralize acid and form a salt.
Ammonia (NH3) neutralizes HCl in the stomach.

59
Q

Functional Groups

Definition and 4 common functional groups

A
  • *Functional Groups**: groups of atoms at occur frequently in organic substances. They greatly influence the properties of the molecule
  • *Carboxyl group** –COOH. Acts as an acid realizing H+ to become r-COO-. Fatty acids and amino acids.
  • *Amino group** –NH2. Can accept or release H+ depending on pH. Can form bonds with other molecules. Amino acids
  • *Hydroxyl group** –OH. May link molecules through dehydration synthesis. Hydrogen bonding between hydroxyl groups and water molecules affect solubility. Carbohydrates, fatty acids, amino acids.
  • *Phosphate group** –PO4. May link other molecules to form larger structures. May store energy in high-energy compounds. Phospholipids, nucleic acids and high-energy compounds.
60
Q

Carbohydrate

A

An organic compound containing carbon, hydrogen and oxygen in the ratio 1:2:1. Includes sugars and starches.
Function: Energy sources that are catabolized rather than stored.

61
Q

Monosaccharide

Disaccharide

Polysaccharide

A

Monosaccharide: simple sugar. A carbohydrate containing 3-7 carbon atoms.
• Glucose (C6H1206), the most important metabolic fuel in the body.
• The atoms can form a straight chain or a ring, which is more common in the body.
• Dissolve readily in water and are rapidly distributed throughout the body by blood and other bodily fluids.
Disaccharide: Two monosaccharides joined together. They cannot be absorbed by the body. They need to be disassembled by hydrolosys before they can provide useful energy.

Polysaccharide: Complex carbohydrates formed by the addition or monosaccharides and disaccharides by dehydration synthesis.
Glycogen: animal starch; has many side branches consisting of chains of glucose molecules. Does not dissolve in water or other body fluids. Muscle cells make and store glycogen.

62
Q

Isomer

A

The 3-dimensional structure of a molecule is important because it usually determines the molecule’s fate or function.
Isomers: molecules with the same types and numbers of atoms but a different structure.
Glucose, Fructose and Galactose are isomers.

63
Q

Lipids

A

Organic molecules containing Carbon, Hydrogen and Oxygen with a ration of 1:2 but a much lower proportion of Oxygen. Fats, oils and waxes.
• Lipids provide twice as much energy as carbohydrates, gram per gram.
• 12-18% of body weight in men and 18-24% in women.
• 5 types: Fatty acids, Eicosonoids, Glyderides, Steroids, phospholipids and glycolipids.

64
Q

Fatty Acids

A

Long chains of carbon atoms with hydrogen atoms attached. One end of the carbon chain is attached to a carboxyl group. Amphipathic – Hydroxyl group is hydrophyllic.
Energy source: Lauric acid.
Saturated: 4 single covalent bonds.
Unsaturated: at least one single covalent bond is replaced by a double covalent bond
Monounsaturated: one double covalent bond
Polyunsaturated: more than one double covalent bond.

65
Q

Eicosonoids

A

Lipids derived from arachidonic acid, which cannot be synthesized by the body.
Leukotrines and Prostoglandins.
Chemical messengers coordinating local cell activity

66
Q

Glycerides

A

Fatty acids strung together by a simple sugar, glycerol, using dehydration synthesis.
Monoglyceride: glycerol and one fatty acid
Diglyceride: glycerol and two fatty acids
Triglyceride: glycerol and 3 fatty acids
Energy source
Insulation – fat under skin
Protection – cushions organs
• Adipose tissue
• Absorbs lipid soluble vitamins (A, E, K)
• raises ldl of cholesterol. Normal <150. High >200

67
Q

Steroids

A

Lipid molecules that share a distinctive carbon framework.
Cholesterol.
Maintains cell membranes
Regulation of sexual function
Regulation of tissue metabolism and mineral balance. (calcitriol and corticosteroids)
Bile salts required for normal processing of dietary fats.

68
Q

Phospohlipids and Glycolipids

A

Amphipathic lipids responsible for membrane function. Called structural lipids.
Phospholipids: A phosphate group links a diglyceride to a non lipid group.
Glycolipids: A diglyceride is attached to carbohydrate.

69
Q

Proteins

A

Formed from hundreds or thousands of amino acids linked together by peptide bonding.
• They are the most abundant organic compound in the body. 20% of body weight.
• All proteins contain Carbon, Oxygen, Hydrogen and Nitrogen.

Structure: create 3-dimensional framework for body
Movement: Muscular contraction
Transport: Transport proteins move various materials from one part of the body to another
Metabolism: Enzymes accelerate chemical reactions in cells
Buffering: Help prevent dangerous changes to PH
Control and coordination: of metabolic activity of cells
Defense: antibodies and clotting proteins

70
Q

Peptides

A

Amino acids linked together by a peptide bond
Peptide Bond: Dehydration synthesis creates a covalent bond between the carboxyl group of on amino acid and the amino group of another

71
Q

Protein Shape

A

Primary Structure: The structure of amino acids along the length of a single polypeptide.
Secondary Structure: Results from the bonds between atoms at different parts of the polypeptide chain. Can create an alpha-helix or a pleated sheet.
Tertiary Structure: Results from the interactions between the polypeptide chain and the surrounding water molecules.
•Complex coiling and folding that gives the protein its final 3-dimensional shape.
** Quartenary Structure**: The interaction between individual polypeptide chains to form a protein complex.

Fibrous Proteins: Long strands or extended sheets.
• They are usually the product of secondary structure or quartenary structure.

• Tough, durable and insoluble in water.

• Keratin and collagen.
Globular Proteins: Compact, rounded and generally enter aqueous solutions.
• Generally a product of the tertiary structure
• Can only function if they remain in solution

72
Q

Functioning of a Protein

A

The shape of a protein determines its functional properties. The sequence of amino acids is responsible for shape.
• Tertiary and quartenary shapes depend not only on amino acids, but also on environmental conditions. Ionic composition, temperatures and pH of surroundings can affect the functioning of a protein.

73
Q

Enzymes

A
  • *Enzymic Function:** Almost everything that happens in the body does so because a specific enzyme makes it possible.
  • *Substrates**: Reactants in an enzymatic reaction.
  • *Active Site**: The place where substrates can adhere to the enzyme
  • *Cofactor**: An ion or molecule that must bind to the enzyme before substrates can also bind.
  • *Coenzyme**: Non-protein organic molecules that function as cofactors. Vitamins.
  • *Isozyme**: 2 enzymes that can catalyzye the same reaction.
74
Q

3 Characteristic of Enzymes

A

Specificity
Saturation Limits
Regulation (active and inactive under different conditions)

75
Q

Denaturation

A

A change in tertiary or quartenary structure of a protein due to temperature and pH that makes it nonfunctional.

(Frying an egg)

76
Q

Nucleotides

A

Individual subunits of nucleic acids.
• A pentose (ribose for RNA and deoxyribose for DNA) attached to both:
• A phosphate group

• A nitrogen base (adenine, guanine, cytosine, thymine, uracil)

  _Purines:_ double ringed bases. Adenine and Guanine

  _Pyramidines_: single ringed bases. Thymine, Cytosine, Urine.
77
Q

Nucleic Acid

A

The primary role of nucleic acids is the storage and transfer of information – specifically, information essential to the synthesis of proteins within our cells.
Formed by dehydration synthesis attaching the phosphate group of one nucleotide to the sugar of another.

78
Q

DNA Molecule

A
  • *DNA Molecule:** Consists of a pair of nucleotide chains. Hydrogen bonding between opposing nigtrogenous bases holds the two strands together.
  • *Complementary base pairs:** The combinations of nitrogen bases: AT, CG.
  • *Complementary Strands:** The two nucleotide strands
79
Q

High-Energy Compound

A

A high energy bond connects a phosphate group to an organic molecule.
AMP – nucleotide Adenosine monophospate.
ADP- Adenosine diphosphate (AMP plus another phosphate group)
ATP-Adenosine triphosphate (ADP plus another phosphate group)

80
Q

What Enzyme is needed to convert ADP to ATP and why is it important?

A

The conversions of ADP to ATP is the most important method of energy storage in our cells. The reversion of ATP to ADP is the most important method of energy release.
The conversion of ADP to ATP requires the enzyme: ATPase

81
Q

Nitrogen Bases

A

Nitrogen Bases: Eventually become our chromosomes.
Purines: double ringed bases. Adenine and Guanine
Pyramidines: single ringed bases. Thymine, Cytosine, Urine.

82
Q

RNA vs. DNA

A

RNA vs. DNA:
RNA: Adenine, Uracil, Guanine, Cytosine. DNA: Adenine, Thymine, Guanine, Cytosine
100-50,00 nucleotides >45million nucleotides
Shape varies (mRNA, tRNA, rRNA) Paired strands coiled in a double helix
Performs protein synthesis as directed by Stores genetic info that controls protein
DNA Synthesis

83
Q

Phosphorylation

A

Adding a phosphate group to ADP with a high-energy bond to form the high energy compound ATP.

84
Q

Glycolosis

A

The anaerobic breakdown of glucose into 2 3-carbon molecules of pyruvate. The molecules are absorbed by the mitochondria with a net gain of 2 ATP molecules.

85
Q

Centrosomes and Centrioles

A

Cytoplasm contains 2 centrioles at right angles.
Each centriole is made of microtubules in a 9+0 arrangement.
They are in 9 groups with 3 in each group.
Essential for movement of chromosomes during cell division.
Centrioles form the spindle apparatus associated with the movement of DNA strands.

86
Q

Nucleus of a cell

A

Largest part of the cell.
Control of metabolism
Storage and processing of genetic information.
Contains DNA of cells – instructions for protein synthesis

87
Q

Mitochondria

A

Mitochondria: Has its own DNA
Make ATP from 3carbon sugars broken down by glycolosis.in the cytoplasm.

citirc acid cycle.

88
Q

Cillia

A

Long extensions containing microtubules in a 9+2 array.
Moves material over cell surface
Flagella are bigger and longer but do the same for sperm.
Problems in respiratory system. Smoking and alcohol affect the length of the Cillia and they can’t move pathogens out of the system.

89
Q

Ribosomes

A

RNA and proteins.
Fixed ribosomes are attached to RER and make proteins for secretion
Free ribosomes are in the cytoplasm and make proteins for use by the cell.
Both types synthesize protein by using instructions provided by mRNA

90
Q

Golgi Apparatus

A

Stacks of flattened membranes containing chambers.
Modification and packaging of chemical reactions.
Storage alteration and packaging of secretory products and lysosomal enzymes.
Defective Golgi- Tcell disease.

91
Q

Lysosomes

A

Vesicles containing digestive enzymes.
Intracellular removal of damaged organelles and pathogens
Controls cholesterol level
LSD- lysosomal storage diseases – lack of specific lysosomal enzymes results in the build up of waste products and debris in the cells. Vital cells can no longer function.

92
Q

Microvilli

A

Membrane extensions containing microfilaments.
Increases surface area to facilitate absorption of extracellular materials.

93
Q

Endoplasmic Reticulum

A

– Rough and smooth.
Rough: Modifies and packages newly synthesized proteins.
Smooth: Synthesizes lipids and carbohydrates
Detoxification – Kidneys and liver
Stores calcium

94
Q

Plasma Membrane Functions

A

Plasma Membrane Functions: (Cell Membrane):
Barrier: Physical isolation
Regulation: what comes in and goes out of cell
Monitors: extracellular fluid and chemical signals
Structural support- anchors the cell

95
Q

Plasma Membrane Componants

A

Lipids: Phospholipid bylayer. Hydrophillic heads on the outside and hydrophobic tails on the inside.
Provides a barrier to ions and water.
Carbohydrates:
Proteoglycans, glycoproteins and glycolipids
Extend outside the cell membrane.
Form sticky ‘sugar coat’ - Glycocalix
Lubrication and protection
Anchoring and locomotion
Specificity in binding (receptors)
Recognition (immune response)
Proteins:
Integral Proteins: within the membrane
Peripheral Proteins: bound to inner or outer surfaces of the membrane.
Anchoring Proteins: attach to the inside or outside structures
Recognition Proteins: label cells as normal or abnormal
Enzymes: catalyze reactions
Receptor Proteins: Bind and respond to Ligands (ions, hormones)
Carrier Proteins: Transport specific solutes through membrane
Channels: Regulate water flow and solutes through membrane.

96
Q

Contents of Nucleus

A

DNA – all information to build and run organisms
`Nucleolus: protein synthesis.
Made of RNA, enzymes and histones
Synthesize rRNA and ribosomal subunits.
Nuclear pores: important during cell division so mRNA can enter nucleolus to retrieve instructions for protein synthesis from DNA.
Nucleosomes: DNA coiled around histones.
Chromatin: Loosely coiled DNA (cells not dividing)
Chromosomes: Tightly coiled DNA (cells dividing)
Chromatid: Each strand of the double-stranded chromosome

97
Q

Information storage in the Nucleus

A

DNA: Instructions for every protein in the body
Gene: DNA instructions for one protein
Genetic code: The chemical language of DNA instructions
Sequence of bases on a strand
Triplet code: 3 bases=1 amino acid

98
Q

Role of Gene Activation in Protein Synthesis

A

The nucleus contains chromosomes
The chromosomes contain DNA
DNA stores genetic instructions for proteins
Proteins determine the cell structure and function.

99
Q

Protein Synthesis

A

Transcription: 3 Steps
copies instructions from DNA to mRNA (in nucleus)
Gene activation
Uncoils DNA, removes histones
Start and Stop codons (promoters and terminators) locate the gene
Coding Strand: code for protein
Template Strand: Used by RNA polymerase molecule
DNA to mRNA
Enzyme RNA polymerase transcribes DNA
Binds to promoter
Reads DNA Code for gene
Binds nucleotides to form mRNA
mRNA duplicates DNA coding strand – uracil replaces thymine.
RNA processing
At stop signal, mRNA detaches from DNA molecule
Code is edited (RNA processing)
Unnecessary codes (introns) removed
Good codes (exons) spliced together
Triplet of three nucleotides (=1 amino acid)

Translation:
mRNA moves from the nucleus through a nuclear pore -
to a ribosome in the cytoplasm surrounded by amino acids
mRNA binds to ribosomal subunits
tRNA delivers amino acids to mRNA
tRNA anticodon binds to mRNA codon
1 mRNA codon translates to 1 amino acid
Enzymes join amino acids with peptide bonds
At stop codon, components separate.

100
Q

How Nucleus Controls Cell Structure and Function

A

Direct control through synthesis of
Structural proteins
Secretions
Indirect control over metabolism through enzymes.

101
Q

Passive Transport

A

no energy expenditures
Potential and kinetic energy

Diffusion

Osmosis

Facilitated Diffusion

Filtration

102
Q

Diffusion

A

Net movement of substances from higher concentration region to lovwer concentration region without energy expenditures.
Movement: Brownian Random Motions of movement until equilibrium is reached.
Factors affecting Diffusion:
Size of particles
Concentration- low concentration→low rate /high concentration→high rate
Solubility- more lipid, higher solubility – things move faster in lipid environment because lipids are non-polar
Molecular weight: lighter molecules→higher rate
Diffusion through simple squamous epithelium

103
Q

Osmosis

A

Net movement of substances from a higher concentration region to a lower concentration region through a semi-permeable membrane
Facilitated by aquaporines.
Osmotic pressure stops osmosis – created equilibrium
Albumin – the plasma protein responsible for osmotic pressure. (most abundant plasma protein in body)
Important for regulating water content.

104
Q

Tonicity

A 
Tonicity: ability to regulate cell volume.
 Don’t want to saturate the system with too much water → water intoxication
 Hormone ADH (antidiuretic hormone) regulates water level.
105
Q

Isotonic Fluid

Hypotonic Fluid

Hypertonic Fluid

A

Isotonic fluid: (saline) physiological solutions) represented by watner content in system
Concentration in cytoplasm 0.9% NaCL
Net movement in that solution is equal – same amount enters and leaves
Preserve things in itsotonic environment.
Hypotonic fluid: <.85%NaCl
Net movement→ goes in faster than it comes out.
Red blood cells in that membrane will break out.
Hemolysis→ blood will spill out and cell dies
Use for treatment → replacing salts and electrolytes
Gatorade
Hypertonic fluid: >.9%NaCl
Water moves out faster than it moves in.
Cell shrinks (crenates) – plasmosis
Use for treatment → head injury
Take fluid out – release pressure of swelling.

106
Q

Facilitated DIffusion

A

Movement of any substance from a high concentration to a low concentration with a carrier protein.

107
Q

Filtration

A

Movement of substance from high concentration to low concentration with
hydrostatic pressure.
Kidneys process our waste with filtration

108
Q

Active Transport Mechanism

A

Movement for a low concetration to a high concentration
Movement against concentration gradient
Requires carrier protein or molecule
Primary Active transport:
Sodium potassium pump
1 molecule ATP to move 3 sodium out and 2 potassium in
without sodium the membrane will depolarize
Membrane is more permeable to k than to Na

Anatomy and Physiology 1 (2 decks)

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