Renin: Difference between revisions
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[[Image:ColoredRenin.png|thumb|530px|alt=text|Renin]] | [[Image:ColoredRenin.png|thumb|530px|alt=text|Renin]] | ||
Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site to specifically cleave peptide substrates using an acid-base hydrolysis mechanism. Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I. | '''Renin''', also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site to specifically cleave peptide substrates using an acid-base hydrolysis mechanism. Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I. | ||
Renin is secreted by the kidneys. The kidneys act both directly and indirectly to regulate arterial blood pressure and provide the major long term mechanism of blood pressure and control. The direct mechanism changes blood volume independently of hormones. When blood pressure and blood volume increase the kidneys can not filter all of the liquids and thus liquids are lost in the urine to decrease blood pressure and blood volume. | Renin is secreted by the kidneys. The kidneys act both directly and indirectly to regulate arterial blood pressure and provide the major long term mechanism of blood pressure and control. The direct mechanism changes blood volume independently of hormones. When blood pressure and blood volume increase the kidneys can not filter all of the liquids and thus liquids are lost in the urine to decrease blood pressure and blood volume. |