1.a&p i intro.2010

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Anatomy & Physiology I-BIO 110Dr. G. Krasilovsky1

Welcome e-mail:

[email protected]

Office hours: after class by appointment

Office: Lecture Classroom!!

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Chapters:

1 - pp.1-11 plus lab material pp12-22

2 - skim pp.29, 42-60

3 - Next Unit:

pp.62-95; 100-105

Readings for Unit IMarieb & Hoehn (2010). Human Anatomy & Physiology. 8th edition.

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UNIT I - Introduction I. Introduction

A. What is Life? B. Physiological Processes C. Directional Terms (lab material) D. Body Cavities (lab material)

II. Chemistry for the Cell

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A. What is Life? 1. A quality or characteristic of a system

that demonstrates the following: a) consists of specific chemicals that can interact

and utilize or produce energy (energy = ability to do work)

b) has an organized basic structure (CELL) which could increase in size and number (ANATOMY = study of structure)

cell = basic unit of structure and function of all living things

tissue = group of cells with similar structure and function

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A. What is Life? b) Basic Structure - continued

-cell = basic unit of structure and function of all living things

-tissue = group of cells with similar structure and function (muscle tissue, connective tissue)

-organ = group of different tissues that function together (stomach, heart, ovaries)

-system = group of different organs that function together (circulatory system, respiratory system)

-organism = a living individual or a group of different systems that function together

c) is capable of relating various physical and chemical processes (PHYSIOLOGY)

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Fig. 1.1

Copyright © 2010 Pearson Education, Inc.

Figure 1.1 Levels of structural organization.

Cardiovascularsystem

OrganelleMoleculeAtoms

Chemical levelAtoms combine to form molecules.

Cellular levelCells are made up ofmolecules.

Tissue levelTissues consist of similartypes of cells.

Organ levelOrgans are made up of different typesof tissues.

Organ system levelOrgan systems consist of differentorgans that work together closely.

Organismal levelThe human organism is made upof many organ systems.

Smooth muscle cell

Smooth muscle tissue

Connective tissue

Blood vessel (organ)

HeartBloodvessels

Epithelialtissue

Smooth muscle tissue

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3

4

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B. Physiological Processes 1. Examples of life processes demonstrating

relationships Several ways to show relationships between

processes- all correctLocomotion (movement)

What systems are involved?

---

Continue adding physiological processes

8Copyright © 2010 Pearson Education, Inc.

Figure 1.2 Examples of interrelationships among body organ systems.

Digestive system Takes in nutrients, breaks them down, and eliminates unabsorbed matter (feces)

Respiratory systemTakes in oxygen and eliminates carbon dioxide

Food O2 CO2

Cardiovascular systemVia the blood, distributes oxygen and nutrients to all body cells and delivers wastes and carbon dioxide to disposal organs

Interstitial fluid

Nutrients

Urinary systemEliminates nitrogenouswastes andexcess ions

Nutrients and wastes pass between blood and cells via the interstitial fluid

Integumentary system Protects the body as a whole from the external environment

Blood

Heart

Feces Urine

CO2O2

Fig. 1.2

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2. Metabolism

a) sum total of all chemical processes in an organism’s cells

b) includes ALL physiological process listed above

c) general term: “metabolic disorder”????? d) indicative of the energy utilization of an

organism and its components: this is the value of metabolic rate

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3. HOMEOSTASIS

a) self regulation of the internal environment of an organism, maintaining life functions within a NORMAL

range b) Examples:

Blood sugar Blood pressure Body temperature Hydration levels / Salt levels, etc.

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Fig. 1.4


Figure 1.4 Interaction among the elements of a homeostatic control system.

Stimulusproduceschange invariable.

Receptordetects change.

Input: Information sent along afferent pathway to control center.

Output:Information sent along efferent pathway to effector.

Responseof effector feeds back to reduce the effect ofstimulus and returns variable to homeostatic level.

Receptor Effector

ControlCenter

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2

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5

BALANCE

Afferentpathway

Efferentpathway

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Figure 1.5 Regulation of body temperature by a negative feedback mechanism.

Sweat glands activated

Shiveringbegins

StimulusBody temperaturerises BALANCE

Information sentalong the afferentpathway to controlcenter

Information sentalong the afferentpathway to controlcenter

Afferentpathway

Afferentpathway

Efferentpathway

Efferentpathway

Information sentalong the efferentpathway toeffectors

Information sentalong the efferentpathway to effectors

StimulusBody temperature falls

ReceptorsTemperature-sensitivecells in skin and brain

ReceptorsTemperature-sensitivecells in skin and brain

EffectorsSweat glands

EffectorsSkeletal muscles

Control Center(thermoregulatory

center in brain)

Control Center(thermoregulatory

center in brain)

ResponseEvaporation of sweatBody temperature falls;stimulus ends

ResponseBody temperature rises;stimulus ends

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Fig. 1.5 modified

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4. Stress - the absence of homeostasis

What are physiological signs of stress? - -

Value of stress vs. stress as a sign of disorder

5. Negative and Positive feedback Ability of an end-product to regulate its own

production

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Figure 1.8 Regulation by feedback mechanisms

See Fig. 1.6 modified

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Fig. 1.6


Figure 1.6 Summary of the positive feedback mechanism regulating formation of a platelet plug.

Feedback cycle endswhen plug is formed.

Positive feedbackcycle is initiated.

Positivefeedbackloop

Break or tearoccurs in blood vessel wall.

Plateletsadhere to site and release chemicals.

Released chemicals attract more platelets.

Platelet plugforms.

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1

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19Fig. 1.9Copyright © 2010 Pearson Education, Inc.

Figure 1.9 Dorsal and ventral body cavities and their subdivisions.

Cranialcavity(contains brain)

Dorsalbodycavity

Vertebralcavity(contains spinal cord)

Cranialcavity

Superiormediastinum

Pericardialcavity withinthe mediastinum

Pleuralcavity

Vertebralcavity

Abdomino -pelviccavity

Ventral bodycavity(thoracic andabdominopelviccavities)

Abdominal cavity(contains digestiveviscera)

Diaphragm

Pelvic cavity(contains urinary bladder, reproductive organs, and rectum)

Thoraciccavity(containsheart andlungs)

(a) Lateral view (b) Anterior view

Dorsal body cavityVentral body cavity

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II. Chemistry for the Cell (pages 42 - 60)

A. Definitions 1. Element - simplest form of matter 2. Chemical Compound - 2 or more

different elements in definite proportion H2O HCl C6H12O6

H2O2

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•3. Monomer - basic repeating building blockindividual bricks, stones, tiles

4. Polymer - many monomers joined together = wall, path, ceiling or floor

Organic compounds are carbon containing complex compounds or polymers

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B. Table of Organic compounds

1. Carbohydrates (C O H) 1a. Monomer = Monosaccharides 3 carbon / 5 carbon / 6 carbon=hexose Hexose = C6H12O6

Glucose or Fructose or Galactose Isomers - same number and type of elements but

different structural arrangement Glucose is the most important monosaccharide

Main source of energy for cell Form glucose from other organic compounds Store glucose as glycogen in animals

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Fig. 2.15a

Glucose Fructose Galactose Deoxyribose Ribose

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•1b. Disaccharide = 2 subunits/monomers

Mono + Mono = Disaccharide + Water Monosaccharides are stable - do not want to react -

make unstable by removing the components of water (HOH) - water is therefore an end product as two monomers bond together

DEHYDRATION SYNTHESIS to produce a larger organic compound (removal of water)

Examples (different monomer combinations) Sucrose=common table sugar Lactose = milk sugar Maltose = malt sugar

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Monomers are joined by removal of OH from one monomerand removal of H from the other at the site of bond formation.

(a) Dehydration synthesis

Figure 2.14a Biological molecules are formed from their monomers or units by dehydration synthesis and broken down to the monomers by hydrolysis reactions.

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Figure 2.14b Biological molecules are formed from their monomers or units by dehydration synthesis and brokendown to the monomers by hydrolysis reactions.

Monomers linked by covalent bond

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(b) HydrolysisMonomers are released by the addition of a water molecule,

adding OH to one monomer and H to the other.

Monomer 1 Monomer 2

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Fig.2.14b


Figure 2.14c Biological molecules are formed from their monomers or units by dehydration synthesis and broken downto the monomers by hydrolysis reactions.

Glucose Fructose

Water isreleased

Water isConsumed

Sucrose

(c) Example reactionsDehydration synthesis of sucrose and its

breakdown by hydrolysis

+

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• 1b. Disaccharide (continued)

DEHYDRATION SYNTHESIS to produce a larger organic compound (removal of water)

HYDROLYSIS is the process to breakdown or digest a disaccharide or larger compound by ADDING components of water to the bond between 2 monomers, and break it

Sugar = 10 or fewer monosaccharides together, sweet tasting and soluble in water Artificial sugar vs. artificial sweetener

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•1c. Multiunits = Polysaccharides

100 or more monosaccharides bonded together

Dehydration Synthesis to bond each 2 monomers together

Hydrolysis to digest the polysaccharide into smaller subunits

Larger saccharides are not soluble in water and not sweet tasting

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•1c. Polysaccharides (continued)

Starch - plant storage polysaccharide, we digest starch and produce glucose

Cellulose - plant polysaccharide makes up cell wall, digested by cows and horses but not by humans (fiber in our diet)

GLYCOGEN - animal storage polysaccharide, excess glucose stored as glycogen primarily in muscle and liver

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Fig. 2.15c

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B. 2. Proteins (C O H N)

2a. Monomer - Amino Acids (Fig. 2.17a-e) 20 common different types which all have an amino

group (NH2-) plus an organic acid group (-COOH) attached to a central carbon

plus a single group of atoms called an -R group attached to the same central carbon

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Fig. 2.17d-e

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B. 2. Proteins (continued) 2b. Linkage of amino acids = Peptide

2 a.a. = dipeptide 3 a.a. = tripeptide 2 - 9 amino acids = small peptide Dehydration synthesis - removal of water (HOH)

from the amino and acid groups (on both sides)

Hydrolysis =??

Fig. 2.18

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B. 2b. Peptides (continued) Biological roles of peptides (2-9 a.a.) Neurotransmitters - peptides released by

nerve cells to stimulate or inhibit another nerve cell or a muscle or a gland

Endorphins - natural opiates, runner’s high Enkephalins

Hormones- peptides released by a gland into the circulatory system to stimulate or inhibit a final target organ (gland or other organ)

Hypothalamic releasing hormones Certain pituitary hormones

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B. 2b. Peptides (continued) Ten or more amino acids = Polypeptide Also biologically active

3. Protein a) Introduction

Large polymer = Macromolecules One or more chains of amino acids Total of 100 - thousands of amino acids Many peptide bonds in a chain

b) Protein functions 1. Cell structure - membranes 2. Transport function - in blood and in/out of cell

LDL vs. HDL

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b) Protein functions 3. Muscle contraction due to contractile proteins 4. Receptors - proteins associated with a cell membrane

to control chemical interactions at the level of the membrane (separate from #1)

A key to open a specific lock A specific chemical interacts with a specific receptor

5. Enzyme - biological catalysts Catalyst - regulate (usually speed up) a chemical

reaction without being used up or changed Some enzymes require cofactors (metal/organic) Specific substrates require specific enzymes

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Fig. 2.21Copyright © 2010 Pearson Education, Inc.

Figure 2.21 Mechanism of enzyme action.

Substrates (S)e.g., amino acids

Enzyme (E)

Enzyme-substratecomplex (E-S)

Enzyme (E)

Product (P)e.g., dipeptide

Energy isabsorbed;bond isformed.

Water isreleased.

Peptidebond

1 Substrates bind at active site. Enzyme changes shape to hold substrates in proper position.

2 Internalrearrangements leading to catalysis occur.

3 Product isreleased. Enzyme returns to original shape and is available to catalyze another reaction.

Active site

+

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Figure 2.19 Levels of protein structure.

Secondary structure:The primary chain formsspirals (α- ) helices and

(sheets β- ).sheets

:Tertiary structure .Superimposed on secondary structure

α- / Helices and orβ- sheets are folded up

to form a compact globular molecule held together by intramolecular .bonds

:Quaternary structure , Two or more polypeptide chains each , with its own tertiary structure combine

.to form a functional protein

Tertiary structure ofprealbumin(transthyretin), a protein that

transports the thyroid hormone thyroxine in serum andcerebro-

.spinal fluid

Quaternary structure of a functional prealbumin .molecule

Two identical prealbuminsubunits join head to tail to form thedimer.

Amino acid Amino acid Amino acid Amino acid Amino acid

α- : Helix The primary chain is coiled , to form a spiral structure which is

.stabilized by hydrogen bondsβ- : Sheet The primary chain“zig-zags” back

and forth forming a“pleated” . sheet Adjacent .strands are held together by hydrogen bonds

( ) :a Primary structure The sequence of amino acids forms the .polypeptide chain

( ) b

( ) c

( )d

Fig. 2.19 Levels of Protein Structure

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3. Fats or Lipids a) C-O-H, but different ratio from carbohydrates b) properties - do not mix well with water, but dissolve

in organic solvents Fats = solid Oils = liquid

c) subunits (not monomers) Fatty acids - varying hydrocarbons plus organic

acid Glycerol - same sugar alcohol Triglycerides = 3:1 ratio

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d) Fig. 2.16a

• Dehydration synthesis

• Hydrolysis

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3.d. Types of fatty acid chains

Saturated fats Solid at room temperature Usually animal products All single bonds between carbon -carbon

Straight, packed together = solid Not metabolized as well - come out of solution during

transport in blood - arteriosclerosis Unsaturated Fats

Often liquid at room temperature(not packed) Usually plant products Some carbon=carbon double bonds, therefore fewer

hydrogen attached to carbons, kinks Metabolized and transported better than the above in the

blood Trans fat - oils that are solidified with addition of hydrogen at

double bonds :. Not metabolized well (margarine)

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Fig. 2.16 b-c

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3.e. Functions of Fats/Lipids

1. Protect and insulate body organs Second source of energy for the cells Chief component of cell membrane

structure - phospholipids (Fig. 2.15b) Cholesterol also part of cell membrane

structure (NOT A FAT) Prostaglandins - made from fatty acid

chain, universal in body, involved with blood clotting, inflammation, birth - aspirin inhibits its synthesis

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4. Nucleic Acids (C O H N P) a) monomer = nucleotide with three

components 5 carbon sugar = pentose Phosphate Nitrogen containing base (1 of 4 types) Fig. 2.22a

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Fig. 2.23


Figure 2.23 Structure of ATP (adenosine triphosphate).

Adenosine triphosphate (ATP)

Adenosine diphosphate (ADP)

Adenosine monophosphate (AMP)

Adenosine

Adenine

Ribose

Phosphate groups

High-energy phosphatebonds can be hydrolyzedto release energy.

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4. Nucleic Acids (Fig. 2.22b)

b) Polynucleotide Dehydration

synthesis Hydrolysis

c) 100 - 1000s of nucleotides equals a Nucleic Acid DNA - Deoxyribose

Nucleic Acid RNA - Ribonucleic

AcidCopyright © 2010 Pearson Education, Inc.

Figure 2.22b Structure of DNA.

DeoxyribosesugarPhosphate

Sugar-phosphatebackbone

Hydrogen bond

Adenine (A)

Thymine (T)

Cytosine (C)

Guanine (G)

(b)

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3 black underlined comparisons most important

1.a&p i intro.2010

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