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Anatomy & Physiology I-BIO 110Dr. G. Krasilovsky1
Welcome e-mail:
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
Copyright © 2010 Pearson Education, Inc.
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
1
2
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5
BALANCE
Afferentpathway
Efferentpathway
12Fig. 1.5
Copyright © 2010 Pearson Education, Inc.
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
Copyright © 2010 Pearson Education, Inc.
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
3
4
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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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Copyright © 2010 Pearson Education, Inc.
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
+
(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
Copyright © 2010 Pearson Education, Inc.
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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Copyright © 2010 Pearson Education, Inc.
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
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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