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INSULIN
Regulates the amount of glucose in the body.

STRUCTURE: Composed of 2 polypeptide chain o Chain A 21 Amino Acids o Chain B 30 Amino Acids On secondary structure: Coiling of amino acid residues forming short sections of - helix o H- bond between N-H and C-O group (terminal group) that stabilizes the structure o Other amino acids compacts the overall structure 3 Disulfide bridges in the cysteine amino acid o Effects on changes on the secondary structure because disulfide bridges are also involved in the formation of the loops of the backbone o Gives stabilization to the tertiary and quarternary structure o The interchain disulfide bridges are absolute conditions for quarternary structure to exist In the quarternary structure: o Cysteine residues play important role in catalytic process of enzymes in storage and adjusting the reduction potentials. o Toroidal ( doughnut shape) form which insulin is stored in - cells and secreted in the bloodstream o Insulin can form into granules consisting of hexamers *Hexamer- combination of proinsulin and insulin both combine with zinc Disulfide bridges is one of the most important part in the structure o Necessary for protein to carry out its function o Without disulfide bridges there will be decrease in binding with the IGF receptor *IGF receptor- receptor attach to the IGF (Insulin like Growth Factor) hormone * IGF (Insulin like Growth Factor) hormone-A hormone produced by liver DIABETES

stimulated by GH (Growth Hormone) that is responsible for cell movement growth and reproduction. Insulin Is a Heterodimeric Polypeptide o Substitutions occur at many positions within either chain without affecting bioactivity and are particularly common in positions 8,9 and 10 of the A chain. Thus, this region is not crucial for bioactivity o Several positions and regions are highly conserved in mammalian specie except: Location of 3 disulfide bridges N-C terminal regions of the A chain

Glucose is unable to enter the cells from the pancreas when the sugar levels are too low Type 1 Diabetes- Insulin Independent Diabetes Mellitus (IDDM) o Exist due to damaged - pancreatic cells and unavailability to excrete insulin in normal way

Type 2 Diabetes Non- Insulin Dependent Diabetes Mellitus (NIDDM) o Pancreatic - cells function perfectly, sometimes over secreting insulin, but tissues around remain unaffected by it Related to obesity

Gestational Diabetes- Diabetes occurring only to pregnant women though as a result of problematic insulin secretion

GLUCAGON
Produced in the islets of Langerhans but by different cells than those that produce insulin. Raises the level of glucose in the blood. Normally secreted between meals to maintain the concentration of glucose in the blood. A single-chain polypeptide containing 18 amino acids and 29 amino acid residues. The liver is more responsive to glucagon Glucagon increases glucose levels in the blood by stimulating the breakdown of glycogen (glycogenolysis) in the liver into glucose which leaves the liver cells and enters the blood stream. 19-22 amino acid sequence is responsible for lipolysis wherein lipolysis is the breakdown of fats. 24-49 amino acid sequence is necessary for glycogenolytic and insulinogenic actions. Glycogenolysis is the breakdown of glucose and Insulinogenesis is the formation and release of insulin by the islets of Langerhans.

REGULATORY PROTEINS (HORMONES) & STRUCTURAL PROTEINS (KERATIN, ELASTIN, COLLAGEN)

The cAMP (Cyclic adenosine monophosphate) generated activates phosphorylase, which enhances the rate of glycogen degradation while inhibiting glycigen synthase and thus glycogen formation.

STRUCTURE OF GLUCAGON

Vasopressin is composed of 9 amino acids (nonapeptide) carries an incomplete electron orbital which makes it able to participate in H-bond reactions a hydrophilic molecule and can travel freely in the blood and will bind to a carrier protein to travel along axons. Cys1 and Cys6 form a disulfide bond. The disulfide bond is responsible for the cyclic structure. The bond works as an important regulator of fluid and electrolyte homeostasis through its anti-diuretic action in the kidney and also participates in the regulation of blood pressure via its potent vasoconstrictor effect. The cyclic structure increases the content of factor VIII (a blood clotting protein) in the blood to prevent excessive bleeding when a blood vessel is injured. Vasopressin contains a basic amino acid, which is Arginine, at position 8. The chemical nature of this amino acid residue is thought to be of critical importance in the interactions of the peptides with their respective receptors. The absence of glycine in side chain causes a decrease in the rate of fibronolysis (process that prevents blood clots from growing)

VASOPRESSIN
Released from the hypothalamus on the posterior pituitary and is transported by the blood to specific receptors. Plays an important role in the water balance of the body. It stimulates reabsorption of water by the kidney, thus having an antidiuretic effect. Maintains proper osmotic concentration of the blood plasma and controls blood pressure through regulating the contraction of smooth muscles. More water is retained, and the blood pressure increases. The secretion of this is increased during hemorrhage. The hormone is destroyed as soon as its function is over and is excreted out along with the urine. Alcohol inhibits the secretion of vasopressin thereby causing dieresis (increased in production of urine) Insufficient secretion of ADH causes diuresis or diabetes insipidus. Such individuals consume large quantity of water to compensate for the excessive loss of water in urination.

SOMATOSTATIN (SS)
aka SRIF (somatotropin release-inhibiting factor) Discovered in hypothalamic extracts. A polypeptide hormone that inhibit the secretion of other hormones such as growth hormone, insulin, glucagon, thyrotropin, gatrin, etc. The action is always inhibitory

Structure and Synthesis Somatostatin is synthesized as 116 amino acid preprohormone that is subsequently cleaved into 2 forms: SS-14 14 amino acids SS-28 28 amino acids

The structure of Vasopressin

REGULATORY PROTEINS (HORMONES) & STRUCTURAL PROTEINS (KERATIN, ELASTIN, COLLAGEN)

Two cysteine residues - allow the peptide to form an internal disulfide bond A disulfide bond maintains the cyclic structure. LYS4 a basic side chain in this position in not essential for gastric activity. TRP8 the precise role could be an involvement in the binding of SS to its receptors. LYS9 more critical than LYS4 for Somatostatins gastric activity. PHE6, PHE7, TRP8, and LYS9 are required for the ion transport and other biologic actions of SS. THR10 serves as an essential spacer. Alteration at PHE11 or LYS4 yields analogs that are selective for ion transport.

collagen found in the linings of your body organs, called basement membranes, and vertebrae of your spine, also called the lamina. FUNCTION Each specific type performs a different function. Some function on their own while some types function in a supporting role. The most important overall function of collagen is to strengthen, support and provide elasticity to your skin. Another important function is to provide flexibility, support and movement in cartilage tissues, such as cartilage in your ears, nose, knees and parts of your larynx and trachea. Collagen also functions as a protective covering for body organs such as the kidneys and spleen. Some types of collagen function to strengthen tendons and ligaments. STRUCTURE Collagen type determines its structure and ultimately, its function. Differing amino acid arrangements result in structures such as Type l thick fibrils and fibers, Type ll thin fibrils and Type lll medium-sized fibrils. Factors such as ultraviolet rays of the sun or the lightbulbs used in tanning booths, free radical cells, problems relating to glucose metabolism and effects of smoking can cause changes to the structure of collagen. Collagen damage is one factor relating to the appearance of sagging skin and skin wrinkles. SYNTHESIS Until you reach approximately 40 years of age, your body consistently produces collagen. After this time, collagen levels start to decline. By the time you reach approximately 60 years of age, all types of collagen are present in greatly reduced amounts. Factors that result in damage to collagen molecules can speed up the decline of overall collagen levels.

Additional info: SS-14 is identical to the carboxyl terminal 14 a.a of SS-28 Production amount depends upon the tissue they are being secreted in. SS-14 is secreted in the pancreas, hypothalamus and regions of nervous system. SS-28 mostly secreted in the intestines, specifically in the Gastrointestinal tract (GI Tract). SS-28 is roughly ten-fold more potent in inhibition of growth hormone secretion, but less potent that SS-14 in inhibiting glucagon release.

COLLAGEN
Collagen is a diverse and multi-talented protein found in both humans and animals. Although a common definition of collagen usually includes the phrase connective tissue, this definition barely scratches the surface of its true function and potential. You can find collagen in a variety of forms, performing a variety of functions, from the top of your head to the tips of your toes and almost everywhere in between. IDENTIFICATION The collagen molecule is a protein made up of 3,150 amino acids arranged in a combination of three strands called a triple helix. The type of amino acid, most often lysine, proline, hydroxylysine or hydroxyproline, along with its arrangement in the helix, determines its function and location in your body. According to Celleraterx.com, collagen is present in 30 percent of your body tissue and 70 percent of your skin tissue. LOCATION Your body contains more than 22 types of collagen, grouped according to physical structure. These types determine where you can find collagen in your body. Seven types are recent discoveries and their specific function is still unknown, according to Celleraterx.com. Types l through V are generally the most prevalent. Type l is collagen found in your skin, bones, tendons, teeth and in scar tissue. Type ll is collagen found in cartilage and a clear gel substance in your eyeball called the vitreous humor. You can find Type Ill collagen in cells of the skin, muscles, blood vessels and lungs. Type lV collagen is intracellular

ELASTIN
is a protein that is elastic and allows many tissues in the body to resume their shape after stretching or contracting, the other name for elastin is tropelastin rich in hydrophobic amino acids containing lysine, valine, alanine and proline residues. Tropoelastin is highly cross link to form an insoluble complex the most common interchain cross link in elastin is the result of the conversion of the amine groups of lysine reactive aldehydes by lysyl oxidase these results in the continuous formation of desmosine cross link. one genetic type no triple helix; random coil conformations permitting stretching no (GLY X- Y) repeating structures no hydroxylysine no carbohydrate intramolecular desmosine cross-links no extension peptides present during biosynthesis

KERATIN
is the primary fibrous structural protein component of hair, skin and nails. Keratin have large amounts of the sulfur containing amino acids: cysteine required for the disulfide bridge that give additional strength and rigidity by permanent. Keratin intermediate filament are also cytoskeletal component of desmosome cellular junction.

REGULATORY PROTEINS (HORMONES) & STRUCTURAL PROTEINS (KERATIN, ELASTIN, COLLAGEN)

Keratin is highly cross link protein typically containing a a helix and b pleated sheets.

OXYTOCIN
Function: Oxytocin stimulates contraction of uterine smooth muscle. It is secreted during labor to effect delivery of the fetus. Oxytocin also stimulates contraction of smooth muscle in the mammary glands (myoepithelial cells). Oxytocin causes smooth muscle contraction in the alveoli (small chambers) and larger sinuses of the mammary glands to make readily available milk, whose production has been induced by prolactin and estrogen, to the suckling infant. Oxytocin causes milk ejection, which is necessary for adequate lactation, but not milk production. Prolactin controls milk production in conjunction with estrogen Structure:

Oxytocin has nine (9) amino acids. Each has Cysteine residues at amino acid positions 1 and 6. These cysteine residues form a disulfide bond with one another to create a cyclic six amino acid ring with 3 amino acid residues hanging off. oxytocin share 7 amino acids in common and differ only at amino acid positions 3 and 8. Oxytoxin is Isoleucine-3, Leucine-8

REGULATORY PROTEINS (HORMONES) & STRUCTURAL PROTEINS (KERATIN, ELASTIN, COLLAGEN)