presentation musculoskeletal health nursing

musculoskeletal

1. I START WITH THE GREATEST NAME OF ALLAH WHO IS REHMAN UR RAHEEM

2. CONTENT Review the digestion and absorption of protein. Explain the significance of nitrogen balance. Describe the synthesis of protein. Discuss the transamination, deamination and decarboxylation. Discuss the formation of urea and ammonia diposal.

3. Daily adult protein requirement is 0.5 – 0.7 kg. For children (1-4 year) protein required is 3-4g/kg. SOURCE OF PROTEIN There are two sources of protein which are:- Endogenous source : (protein forms with in the body). Exogenous source : (Dietry intake of protein). Digestion And Absorption Of Protein

4. DIGESTION OF PROTEIN Protein First starch Pepsin Proteases , Peptones , Polypeptide Trypsin , Chemotrypsin , Carboxypolypeptides From Pancreatic Juice Peptides Small Intestine Peptidsea Aminoacid

5. Digestion of protein starts from stomach. Stomach release pepsin enzyme (pH 2-3) on protein which convert protein into proteases, peptones, polypeptide. Then this food moves into small intestine, where from pancreas enzymes named trypsin, chemo trypsin, are released. It’s convert into peptide. Small intestine release peptides, which convert peptide. Explanation Of Digestion

6. Absorption Of Protein End product of protein digestion is Amino acids. Then from small intestine, amino acids are absorbed into blood by two mechanisms which are Secondary Active Transport Facilitated Diffusion

7. Movement of molecules from low concentration in high concentration is called Secondary Active Transport. Energy is required in this transport. Source of energy is other than ATP. Example: Sodium potassium pump are liver. Secondary Active Transport

8. Facilitated Diffusion It is a type of passive transport. Movement of molecules from higher concentration into low concentration through "Transport protein " is called facilitated diffusion.

9. In healthy adult maintaing a constant weight. The intake of nitrogen in food (mainly from protein). The amount excreted from the body (mainly through urine, feces, and sweat). It is an important concept in understanding protein metabolism and overall health NITROGEN BALANCE

10. Occurs when nitrogen intake exceeds nitrogen excretion. This indicates that the body is in a state of growth or repair. where more protein is being synthesized than broken down. This is typical in situations like (muscle growth, pregnancy, or recovery from illness or surgery). Positive Nitrogen Balance

11. Occurs when nitrogen excretion exceeds nitrogen intake. This indicates that the body is breaking down more protein than it is synthesizing. This can happen during periods of (illness, malnutrition, or muscle wasting). Negative Nitrogen Balance

12. Occurs when nitrogen intake equals nitrogen excretion. This suggests that the body’s protein levels are stable. healthy adults who are not in a state of growth or stress. Nitrogen balance helps to assess protein requirements, as it reflects whether the body is getting enough protein for maintenance (repair, and growth). Neutral Nitrogen Balance

13. PROTEIN SYNTHESIS DEFINITION: Protein synthesis is a biological process occurs inside the cells. Protein synthesis is divided into two phases. Transcription. Translation.

14. Transcriptions: DNA ( RNA polymerase) RNA. Transcription is the process by which the information in a gene's DNA is copied into a complementary RNA molecules. During transcription a section of DNA encoding a protein known as gene is converted into a molecule called messenger RNA (mRNA) this conversion is carried out by an enzyme known as RNA polymerase in the nucleus. There are three steps of transcription. Initiation Elongation Termination

15. Initiation: RNA POLYMERASE BINDING: The enzyme RNA polymerase binds to specific region on the DNA called the promoter the promoter signals of a gene. Unwinding of DNA The DNA helix unwinds in the region of the gene to be transcribed, creating a "bubble" of single stranded DNA .

16. 2: Elongation: RNA polymerase moves along the template strand of the DNA. Reading it in 3' to 5' direction. It synthesizes a complementary RNA strand in the direction 5' to 3'. 1.RNA Synthesis: 2.Base Pairing: The RNA polymerase adds nucleotides to the growing RNA chain. RNA uses Uracil (U) instead of Thymine(T). So A pairs with U and C pairs with G in RNA .

17. 3. Termination : Transcription continues until the RNA polymerase. Reaches a termination signal ( a specific sequence in the DNA). 1.Signal for end: 2.RNA Release: The newly formed RNA strand called messenger RNA. (mRNA) detaches from the DNA template.

18. Translation: Definition: (Translation in the cytoplasm) Translation is the second stage , where the mRNAis used to synthesize a protein. This occurs at the ribosomes in the cytoplasm. There are three sreps of translation. Initiation. Elongation. Termination . The mRNA binds to the ribosomes , and the first tRNA (transfer RNA) carrying an amino acids binds to the starts codon on the mRNA Initiation:

19. Elongation: Termination: The ribosomes readsthe mRNA in triplets (codon) and each codon specifies a particular amino acids. tRNA brings the corresponding amino acids, & the ribosomes links them together to from a growing polypeptide chain. When a stop codon is reached on the mRNA. The ribosomes releases the newly synthesized protein,& the translation process ends.

20. TRANSAMINATION, DEAMINATION AND DECARBOXYLATION Transamination refers to the transfer of an amino group (NH²) from one amino acid to a keto acid, creating a new amino acid and keto acid. Typically involving the enzyme aminotransferase or (transamines). Transamination is a major pathway for converting essential amino acids into non-essential amino acid. The liver is the main site of transamination. All transamination reaction are reversible . Transamination:

21. Examples : Aspartate Transamination : Aspartate donates its amino group (NH²) to α-ketoglutarate. α-ketoglutarate receives the amino group , becoming Glutamate. Aspartate loses its amino group , becoming Oxaloacetate.

22. Deamination : Deamination is the process by which an amino group (NH²) is removed from an amino acid , resulting in the formation of ammonia(NH³) and keto acid. Deamination is an important process in the body as it allows for theremoval of excess amino group & the production of energy through theconversion of amino acids to keto acids. There are two types of deamination:

23. Oxidative Deamination Non-Oxidative Deamination This process removes the amino group from amino acids through oxidation and produces ammonia & carbonyl compound. Oxidative deamination occurs in the mitochondria Oxidative deamination produces α - ketoglutarate . Oxidative deamination only occurs in the liver & kidney. This process removes the amino group from amino acids without oxidation and produces ammonia & α - ketoacids . Non-oxidative deamination occurs in the cytosol. Non-oxidative deamination produces oxaloacetate. Non-oxidative deamination occurs in other types of organisms.

24. Decarboxylation: Decarboxylation is a chemical reaction that removes a carboxyl group (COOH) and releases carbon dioxide (CO²). It usually refers to the removal of a carbon atom from a carbon chain in carboxylic acid.

25. 1 : Ammonia production: 2 : Urea formation: 3 : Urea excretion: FORMATION OF UREA AND AMMONIA DISPOSAL The body produce ammonia when amino acid breakdown. Protein breakdown with the help of protease. The chain of amino acid breakdown when exopeptidase and endopeptidase enzymes act on the chain . Ammonia production:

26. Urea Formation: The liver and mitochondria use enzymes to convert ammonia into urea.

27. Urea Excretion: Urea is synthesized in liver than secreted into bloodstream. Urea taken up by the kidneys for excretion in the urine.