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Physiology > Exam 1 Review- Lectures 1 & 2 > Flashcards

Exam 1 Review- Lectures 1 & 2 Flashcards

1
Q

What is auto regulation and give an example

A

Automatic response in cells, tissue or organs due to changes in the local environment

Ex:

oxygen decrease in tissue so

Cells secrete chemical that dilate blood vessels and increases blood flow and more oxygen to the tissue

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2
Q

What is extrinsic regulation? And give an example

A

The nervous system and endocrine system

As the environment changes there is an electric signal (nervous system) or a chemical messenger (endocrine system) to control or adjust activities of other systems simultaneously

Nervous system- short term, rapid and specific through release of neurotransmitters

Endocrine system- long term, slow and nonspecific using hormones into bloodstream

Ex: exercising
Increase heart is increases blood flow but is reduced in less active organs and given to active muscles

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3
Q

What are the 3 steps in homeostatic regulatory mechanism?

A

1) receptor
2) control center
3) effectors

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4
Q

What is a receptor?

A

Sensor

Receives stimulus or detects environmental change

Sends sensory info to control center through afferent (sensory) pathways

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5
Q

What is the control center?

A

Receives and processes the sensory info supplied by receptor

Sends out commands to effector using the efferent (motor) pathway

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6
Q

What is the effector?

A

Cell or organ that responds to and executes the command sent from the control center

Activity either opposes or enhances the stimulus

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7
Q

True or false for
Homeostatic regulatory mechanism

Limits fluctuations of internal conditions to keep them close to a set point or desired value

A

True

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8
Q

What is negative feedback?

A

It’s the primary mechanism of homeostatic regulation

Proves long term control over body’s internal conditions and systems

Response of effectors negates/ opposes the initial stimulus

Body is brought to homeostasis

Normal range is maintained around a set point

No “normal” physiological values, instead reported as average value or range

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9
Q

What is dynamic regulatory process?

A

Set points varies with changing environment or differing activity levels

Individual variability in homeostatic set points determined by

  • gender
  • age
  • environmental conditions
  • general health
  • genetic factors
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10
Q

What is body temp regulation called?

A

Thermoregulation

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11
Q

What is positive regulation? Examples?

A

Initial stimulus produces an effector response that enhances or increases initial change

Body is moved away from homeostasis (normal range is not maintained)

Found when a potentially dangerous or stressful process must be completed quickly to restore homeostasis

Ex: immediate danger from a severe cut is loss of blood which decreases BP abs reduces heart efficiency so then body forms a blood clot

Labor and delivery

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12
Q

True or false

New chemical bonds form between atoms or existing bonds between atoms are broken

A

True

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13
Q

What is a reactant?

A

Material going in the reaction

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14
Q

What is a product?

A

Material coming out of the reaction

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15
Q

What is metabolism and what does it include?

A

Sum of all biochemical processes occurring within the body at any moment

Includes

  • anabolism
  • catabolism
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16
Q

What is anabolism?

A

Synthesis of new molecules

Forms chemicals bonds

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17
Q

What is dehydration synthesis reaction?

A

AH + BOH —-> AB + H2O

Formation of a complex molecule be removing water molecule

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18
Q

What is catabolism?

A

Breakdown of molecules into smaller fragments

Breaks chemical bonds

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19
Q

What is a hydrolysis reaction?

A

AB + H2O —-> AH + BOH

1 of the bonds in a complex molecule is broken abs components of a H2O molecule (H & OH) are added to resulting fragment

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20
Q

What is water?

A

Polar

Inorganic compounds split into smaller molecules via dissociation in water

Ionization

21
Q

What is ionization?

A

Dissociation into ions

22
Q

After ionization what happens?

A

Ionic bonds are broken as individual ions interact with positive or negative ends of polar H2O molecules

23
Q

What do polar H2O molecules form and why?

A

Hydration spheres around ions and smaller polar molecules

Why?

  • Keep them in solution
  • prevents formation of ionic bonds
24
Q

What is hydrophilic?

A

Water loving

Ionic and/ or polar covalent bonds readily dissolve in water

Ex: glucose

25
Q

What is hydrophobic?

A

Water fearing

Non polar covalent bonds (mostly consisting of C and H) do not dissolve in water

Ex: oils and fats

Body fat deposits consist of large hydrophobic droplets trapped in watery interior of cells

26
Q

What are lipids?

A

Composed of C and H atoms (1:2 ration)

Linked by non polar covalent bonds (hydrophobic)

Important for physio:

  • valuable source of energy
  • major component of cellular membrane
  • signaling molecules
27
Q

What are the 5 subclasses of lipids?

A

1) fatty acids
2) eicosanoids
3) glycerides
4) steroids
5) glycolipids and phospholipids

28
Q

What are proteins

A

~50% or organic material in body (20% of TBW)

Contains C, H, N, O2 and small amounts of S and P

Amino acids are simple organic monomers that combine to form protein polymers

7 function

  • support
  • movement
  • transport
  • buffering actions
  • metabolic regulation
  • coordination and control
  • defense
29
Q

What is the support function of proteins?

A

Structural proteins provide strength, organization and support for cells, tissues and organs

30
Q

What is the movement function of proteins?

A

Contractile proteins bring about muscular contraction

31
Q

What is the transport function of proteins?

A

Transport proteins bind substances in blood including insoluble lipids, respiratory gases and special minerals (iron)

32
Q

What is the buffering action function of proteins?

A

Help prevents dangerous changes in pH of body fluids

33
Q

What is the metabolic regulation function of proteins?

A

Enzymes speed up chemical reactions in cells

34
Q

What is the coordination and control function of proteins?

A

Protein hormones influence metabolic activities of cells

35
Q

What is the defense function of proteins?

A

Keratin- waterproof protein that protects the skin, hair and nails

Antibodies- protect against diseases

Clotting proteins- hemostasis

36
Q

What is an amino acid?

A

Subunit monomers of proteins

Water soluble

Structure:

  • central C
  • H atom
  • amino acid group (-NH2)
  • carboxyl group (-COOH)
  • R group
37
Q

What is an r group?

A

Variable side chain of 1 or more atoms that identifies a specific amino acid

Determine structure and function

Non polar R- hydrophobic
Polar R- hydrophilic
Electrically charged R- strong hydrophilic

38
Q

How do amino acids join together to form a protein?

A

Via Dehydration synthesis

39
Q

How is a peptide bond formed?

A

Covalent bond b/n carboxyl group of 1 amino acid and amino group of another amino acid

40
Q

What are peptides?

A

Molecules consisting of amino acids held together by polypeptide bonds

2 linked amino acids = dipeptide

Tripeptides and larger peptide bonds = polypeptide (ex: hemoglobin, collagen and keratin)

41
Q

What is the secondary protein structure?

A

Results from the H bonding between atoms at different parts of the polypeptide chain

Alpha helix (simple spiral/ coil)

Beta sheet (flat pleated sheet/ parallel)

42
Q

What is the tertiary protein structure?

A

Complex coiling and folding gives a protein it’s final 3-D shape

43
Q

What are the 5 determining factors for the tertiary protein structure?

A
  • H bonds b/n R groups of amino acids or with surrounding water molecules
  • ionic bonds between ionized regions along chain
  • hydrophobic interactions
  • covalent disulfide bonds between sulfur atoms of 2 cysteine amino acids at different sites along chain (strongest bond and create permanent loops or coils in polypeptide chain)
  • van der waals forces (weak abs transient electrical interactions between electrons in outer shells of 2 atoms close to each other)
44
Q

What are enzymes?

A

Catalyst

Proteins that lower activation energy of a chemical reaction

Not changed or used up in reaction

Have substrates

3 enzyme characteristics

45
Q

What are substrates?

A

Reactants

Bind to an active site on an enzyme

H bonding reinforces physical fit

Tertiary or quaternary structure of enzyme determine shape and charge

46
Q

What is specificity of the enzyme characteristics?

A

Catalyze only 1 type of reaction

Due to ability of enzyme sites to bind only to substrates with particular charge or shape

47
Q

What is saturation limits of the enzyme characteristics?

A

Enzymes become saturated (all active sites bound to substrate)

Substrate concentration required to reach max rate of reaction

Higher substrate concentration = faster rate of reaction

Higher enzyme concentration = faster rate of reaction

48
Q

What is regulation of the enzyme characteristics?

A

Active vs inactive

Anything changing the tertiary or quaternary shape of the enzyme can turn it on or off

Important short term control over reaction rates and metabolic pathways

Physiology (7 decks)

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