Anatomy and Physiology 1 Exam 1 UWEC

This is a study set for the Anatomy and Physiology 1 (BIOL214) at University of Wisconsin-Eau Claire, Exam #1, not including all lab information.

Anatomy

the study of structure (shape)

Physiology

the study of function (do)

Inspection

Viewing

Palpation

Feeling

Auscultation

Listening

Percussion

Tapping

Cadaver dissection

Cutting and separating human body tissues to reveal tissue relationships

Comparative anatomy

Study of multiple species to learn about form, function, and evolution

Ways to study anatomy

Exploratory surgery, medical imaging

Medical Imaging

Viewing the inside of the body without surgery/opening the body

Radiology

branch of medicine concerned with imaging

Radiography (X-rays)

Dense tissue appears white

Over half of all medical imaging

**Radiopaque substances**

Injected or swallowed

Fills hollow structures such as Blood vessels and Intestinal tract

__**Computed tomography**__ **(CT scan)**

Formerly called a CAT scan

Low-intensity X-rays combined and computer analysis

**Magnetic resonance imaging (MRI)**

Superior quality to CT scan

Best for soft tissue

Strong magnetic things can make electrons polar until magnet is off, emits radiowaves, hydrogen focused

•__**Positron emission tomography (**__**PET) scan**

Assesses metabolic state of tissue (rate of calorie consumption)

Distinguishes tissues most active at a given moment

Mechanics—inject radioactively labeled glucose

Sonography

•Second oldest and second most widely used

•High-frequency sound waves echo back \n from internal organs

•Avoids harmful X-rays

Gross Anatomy

•Study of structures that can be seen with the naked eye

Histology

•__**(histo=cell/tissues)**__

•Examination of tissues with microscope

Cytology

•**(cyto=cell)**

•Study of structure and function of cells

Hierarchy of Complexity

•**Organism** composed of **organ systems**

•**Organ systems** composed of **organs**

•**Organs** composed of **tissues**

•**Tissues** composed of **cells**

•**Cells** composed of **organelles**

•**Organelles** composed of **molecules**

•**Molecules** composed of **atoms**

Anatomical Variation

**No two humans are exactly alike**

•Anatomy books show most common organization of structures

•Some individuals show __**sitis inversus**__— left-right reversal of organ placement

Characteristics of **Life**

organization, cellular composition, metabolism, responsiveness, movement, homeostasis, development, reproduction, evolution

Characteristics of **Life- organization**

•living things exhibit a higher level of organization than nonliving things

Characteristics of Life- Cellular Composition

•living matter is always compartmentalized into one or more cells (structural and functional unit of life)

Characteristics of Life-Metabolism

internal chemical reactions

Characteristics of Life- Responsiveness

ability to sense and react to stimuli (irritability or excitability)

Characteristics of **Life-Movement**

of organism and/or of substances within the organism

Characteristics of **Life-Homeostasis**

•maintaining relatively stable internal conditions

Characteristics of **Life-Development**

differentiation and growth

Characteristics of **Life-Reproduction**

producing copies of themselves; passing genes to offspring

Characteristics of Life-Evolution

changes in genes from one generation to the next

Aging

all changes occurring in the body with the passage of time: growth, development, and degenerative changes that occur later in life

Senescence

•the degeneration that occurs in organ systems after the age of peak functional efficiency

•Gradual loss of reserve capacities, reduced ability to repair damage and compensate for stress, and increased susceptibility to disease

Senescence of one organ system typically leads to….

senescence of other organ systems. Organ systems do not degenerate at the __**same rate.**__ Some show moderate changes, while others show pronounced differences

How can you slow senescence?

•__**Good nutrition and exercise**__

Resistance exercise (reduces bone fractures)

Endurance excercise reduces body fast and increases cardiac output and oxygen uptake

What is the definable instant of biological death?

There is not one. Some organs function for an hour after heart stops. Brain death is lack of cerebral activity (flat EEG), reflexes, heartbeat, and respiration for 30 minutes to 24 hours. Death usually occurs as a failure of a particular organ followed by a cascade of other organ failures

Negative feedback

•**Negative feedback** allows for **dynamic equilibrium** within a limited range around a __**set point**__

•The response is opposite to the stimulus.

Negative feedback works by:

1. A receptor that senses change in the body.
2. Integrating (control) center which processes the sensory information and makes a decision to direct the response
3. Effector carries out the final corrective action to restore homeostasis

Positive Feedback

•__**Self-amplifying cycle**__

Leads to greater change in the same direction. Feedback loop is repeated, change produces more change. Childbirth is an example.

Gradient

A difference in chemical concentration, charge, temperature, or pressure between two points

•**Matter and energy tend to flow ____ gradients**

down

Heat flows down _______ gradients

thermal

Element

simplest form of matter to have unique chemical properties

Atom

Smallest piece of an element with the chemical and physical properties of the element.

Minerals

__inorganic__ individual elements extracted from soil by plants and passed up food chain to humans​, such as Ca, P, Cl, Mg, K, Na, and S.

Electrolytes

mineral salts needed for nerve and muscle function. substances that ionize in water and form solutions capable of conducting electric current​.

Ion

charged particle (atom or molecule) with unequal number of protons and electron

Ionization

transfer of electrons from one atom to another

Chemical Bonds

hold atoms together within a molecule or attract one molecule to another​

Ionic Bonds

* Attractions between anions and cations (example, NaCl). Electrons donated from one atom to another. Easily broken by water​

Covalent Bond (Non-Polar)

__**Nonpolar bond**__: electrons shared equally (strongest bond) (diatomic)

Covalent Bond: __**Polar bond**__

__**Polar bond**__: electrons shared unequally (spend more time near oxygen) (H2O)

Hydrogen Bond

* a weak attraction between a slightly positive hydrogen atom in one molecule and a slightly negative oxygen or nitrogen atom in another​
* Water molecules are attracted to each other by hydrogen bonds​. DNA and proteins shaped by hydrogen bonds within them​

Molecule

chemical particle composed of two or more **atoms** united by a covalent chemical bond

Compound

molecule composed of two or more different **elements**

Mixtures

* physically blended but not chemically combined​
* Distilling water is physical separation​
* body fluids are complex mixtures of chemicals

Solvency

* ability to dissolve other chemicals​
* Water is called the **universal solvent**

Hydrophilic

* substances that easily dissolve in water​
* Molecules must be polarized or charged (e.g., sugar)​

Hydrophobic

* substances that do not easily dissolve in water​
* Molecules are nonpolar or neutral (e.g., fats)​

Solution

consists of particles called the __**solute**__ mixed with a more abundant substance (usually water) called the __**solvent**__​. Can be gas, solid or liquid. In humans H2O is solvent.

Acid (erroneous definition)

A proton donor (releases H+ ion in water)

Base (erroneous definition)

proton acceptor (accepts H+ ion in water). Many bass release OH-.

pH

a measure derived from the Molarity of H+.

Energy

* capacity/ability to do work​
* To do work means to move something​
* All body activities are forms of work​

Kinetic Energy

* energy of __motion__​
* Example: water flowing through a dam, generating electricity

Potential energy

* energy stored __in an object__, but not currently doing work​
* Example: water behind a dam​

Chemical Energy

potential energy in molecular bonds

Chemical Reaction

* __**Making or breaking chemical bonds.**__ ​
* **Reactions occur when molecules collide with enough force and correct orientation**

**Chemical Reaction rates increase when…**

* Reactants are more **concentrated**​
* **Temperature** rises​
* __**Catalyst**__ is present​

Catalyst

* Enzyme (biological catalysts) bind to reactants and hold them in orientations that facilitate the reaction​
* Lower activation energy needed for reaction​
* Catalysts are not changed by the reaction and can repeat the process frequently​

Organic chemistry

the study of compounds containing __**carbon**__​

**Four categories of carbon compounds**

* Carbohydrates​
* Lipids​
* Proteins​
* Nucleic acids

Macromolecules

very large organic molecules with high molecular weights (appx 1000g amu or more)​

Polymers

macromolecules made of a repetitive series of identical or similar subunits

Polymerization

joining monomers (small) to form a polymer (lots of monomers connected)​

Hydrolysis

digestion/opposite of dehydration synthesis (two monomers coming together).

* The covalent bond linking one monomer to the other is broken​
* The -OH is added to one monomer​
* The -H is added to the other​
* Splitting a polymer by the addition of a water molecule​

**Names of carbohydrates often built from….**

**the root “*****sacchar-*****” or the suffix “-*****ose*****” both meaning sugar, sweet**​

3 IMportant monosaccharides

Glucose, galactose, and fructose, all with the same molecular formula, and all isomers of eachother.

Disaccharide

sugar made of two monosaccharides​

Three important disaccharides​

* **Sucrose**—table sugar​


* **Lactose**—sugar in milk​


* **Maltose**—grain products​

Polysaccharides

long chains of monosaccharides (at least 50)

3 Key Polysaccharides

GLycogen, Starch, Cellulose (not in humans)

Lips are _______ organic molecules

hydrophobic

3 Most significant Lipids

* Triglycerides​
* Phospholipids​
* Steroids​

triglycerides

* Three fatty acids linked to glycerol ​
* Each bond formed by dehydration synthesis​
* Broken down by hydrolysis
* when liquid, called oils (polyunsaturated fats from plants). when solid, called fat (animals)
* Long term energy storage

Trans-Fatty Acids

Two single C-C bonds in **opposite** sides of the C=C double bond

Hard to remove, cause heart disease

Phospholipids

similar to neutral fats except one fatty acid is replaced by a phosphate group​

**Structural foundation**​ **of cell membrane**

Amphipathic

* Fatty acid “tails” are **hydrophobic**​
* Phosphate “head” is **hydrophilic**​
* **Can dissolve in fat and water**​

Steroid

lipid with 17 carbon atoms in four rings​

Cholesterol

* the “parent” steroid from which the other steroids are synthesized​
* Important for nervous system function and structural integrity of all cell membranes​

Protein

* a polymer of amino acids​
* Sometimes called a polypeptide​

Amino Acid (Protein)

* central carbon with three attachments​
* 20 amino acids used to make the proteins are identical except for the radical (R) group​
* Properties of amino acid determined by R group​

Conformation (Protein)

* unique, three-dimensional **shape** of protein crucial to function​
* Proteins can reversibly change conformation and thus function​

Denaturation (Protein)

* Extreme conformational **change** that destroys function​
* Extreme heat or pH​
* Example: when you cook an egg​

**Primary Protein structure** 

* Protein’s sequence of amino acids which is encoded in the genes (Stage 1, beads on a string)​

Secondary protein structure

* Coiled or folded shape held together by hydrogen bonds​
* Most common secondary structures are: ​
* Alpha helix—spring-like shape​
* Beta helix—pleated, ribbon-like shape (beta pleated sheets)​

Tertiary protein structure

* Further bending and folding of proteins primarily due to hydrophobic-hydrophilic interactions (alpha and beta interact with eachother)​

Quaternary protein Structure

* Associations of two or more polypeptide chains due to __**ionic bonds**__ and hydrophobic-hydrophilic interactions ​
* Occurs only in some proteins​
* Example: hemoglobin has four peptide chains​

Protein Functions

Structure, Communication (like insulin), membrane transport (carriers), catalysis (enzymes), recognition/protection (antibodies), movement (motor proteins), cell adhesion (cell binding)