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- un'introduzione sugli amino acidi - digestione delle proteine parlando degli enzimi che aiutano il processo. - "Endopeptidases" e "Exopeptidases" sono spiegati in modo chiaro specificando i loro meccanismi e il loro ruolo nei diversi organi del corpo durante la digestione. - Amino Acid Transport - "Clinical Relevance" e dei problemi che si potrebbero avere se qualche Aminoacido non fosse presente. - catabolismo delle proteine e dei processi metabolici che avvengono, distinguendo di parte in parte (liver, skeletal muscle, kidneys...) - "protein turnover" e affrontare il discorso di "ubiquitin". processi di "Transamination" e "Oxidative Deamination" e degli enzimi più importanti. - ruolo dell'Ammonia (e dell'Urea Cycle) , della Glutamine Synthetase Pathway, del Glucose Alanine Cycle. - Heme Catabolism, Catecholamines, Histamines, Serotonin, Creatine, Melatonine, Nitric Oxide Materia: Biochemistry, primo anno di medicina, professore Luigi Anastasia UniSr
Tipologia: Appunti
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Proteins are involved in nearly every physiological process in the body. They function in various capacities, including: ○ Transport Proteins: e.g. hemoglobinbin (transports oxygen), ferritin (transports iron) ○ Structural Proteins: e.g., elastin and collagen (support the body) ○ Contractile Proteins: e.g., actin and myosin (required for movement) ○ Enzymes: Catalyze numerous biochemical reactions ○ Hormones: Regulate various bodily functions ○ Receptors: e.g., proteins involved in nerve cell transmission ○ Transcription Factors: Regulate gene expression These functions highlight the critical roles of dietary proteins in maintaining human health and physiological processes. AMINO ACIDS IN PROTEINS
Unless you are eating it raw, the first step in digesting an egg (or any other solid food) is chewing. The teeth begin the mechanical breakdown of large egg pieces into smaller pieces that can be swallowed. The salivary glands secrete saliva to aid swallowing and the passage of the partially mashed egg through the esophagus. No protein digestion occurs in the oral cavity. The first phase of protein digestion takes place in the stomach through the action of an endopeptidase, pepsin. Pepsin is a hydrolytic enzyme that attacks the peptide bonds in dietary proteins, specifically those formed by aromatic amino acids such as tyrosine and phenylalanine. We are not really able to store proteins or amino acids! We need to use them for biosynthesis or to convert them into carbon chains that do not contain hydrogen. There are different types of enzymes!! Whole proteins are not absorbed –> they are too large to pass through cell membranes intact. DIgetìstive enzymes. Hydrolases break peptide bonds. They are secreted as inactive pre-enzymes and prevent self digestion. These are all the enzymes that we could encounter. This digestive process requires several steps. ENDO VS EXO PEPTIDASES the key difference is that the endopeptidase breaks peptide bonds within the protein molecules while the exopeptidase cleaves peptide bonds at the terminals of the protein molecules. They start to release progressively the amino acids from the end of the peptide chain and allow to get to the free amino acids. Some are at the N terminus and some are at the C terminus, they will act on different types and shapes of bonds. They need to be secreted in an inactive form as we said.
Pepsin is produced in an inactive form known as pepsinogen by the chief cells of the gastric mucosa. The release of pepsinogen is stimulated by the hormone gastrin in response to HCl. The activation of pepsinogen into pepsin occurs due to the action of HCl in the gastric environment and autocatalytically. This activation involves the removal of a peptide segment from pepsinogen. The low pH will cut the pepsinogen which is longer than pepsin, and pepsin will be activated with the hydrolysis of pepsinogen. A KEY ROLE is played with HCl. How do we synthesize it? https://youtu.be/opWBDkgiWx4?si=d14MmBykgWDl9JEa
Epithelial Cell Activity Brush-Border Peptidases:
•Amino acids cannot be stored but are used for protein synthesis. •Excess amino acids are broken down to produce energy. •After absorption by intestinal cells, amino acids enter the bloodstream (via the portal vein) and are distributed to all cells in the body. IMPORTANT!! not all amino acids are the same, they have different side chains and different structures. They can be essential or non essential. The categorisation of amino acids into their essential, conditional and non-essential groups in humans Conditional amino acids are not usually essential amino acids, only in times of illness and stress. Essential amino acids are not produced naturally by the body and must come from dietary intake whereas non-essential amino acids are produced by our body WHY CAN’T WE MAKE SOME? Humans have lost the ability to synthesize nine essential amino acids due to genetic mutations in our ancestors. These mutations affected enzymes necessary for complex synthesis pathways. The missing enzymes impact the conversion processes shown in the yellow, green, red, and blue boxes on the chart.
NH4+ is either excreted or used in the urea cycle for arginine synthesis.
D-Amino acid oxidase
there are two primary mechanisms by which ammonia is transported to the liver for detoxification and excretion
Elevated ammonia increases glutamate formation, leading to more GABA production in neurons. GABA is an inhibitory neurotransmitter that calms neuronal activity
Kidney