Sandbox Reserved 484: Difference between revisions

Line 7:

[[Image:CTSBFig1.jpg | thumb]]

Cathepsin B is a very complex protein which is a part of the super family of [http://en.wikipedia.org/wiki/Papain papain-like cystein proteases]. These papain-like cysteine proteases are abundant in nature and can be found in baculovirus, eubacteria, yeast, plants, and animals. They are synthesized as inactive ~~pro-enzymes~~ with N-terminal pro-peptide regions. The pro-peptide plays an important role as an inhibitor of enzymatic activity. A number of cysteine proteases are located within lysosomes and they have very specific functions in endo and exopeptidase activity. Cathepsin B is synthesized as a pre-proenzyme of 339 amino acid residues and it can act as an endopeptidase. Its activity is inhibited by a2-macroglobulin. The most crucial functions of Cathepsin B are that it is implicated in the turnover of proteins and carries out different roles in maintaining the normal metabolism of cells. Cathepsin B is found in humans and other mammals and it is encoded by a single gene and this gene exhibits a high degree of sequence homology to other cysteine proteases of the papain super family. However, in parasitic helmiths and free-living nematodes, the cathepsin B genes can be seen as large multigene families instead of just one single gene shown in humans and mammals. The function of this cathepsin B gene has not been verified for sure, but research is showing that cathepsin B could be involved in induction of protective immunity. In diseases, such as cancer and arthritis, Cathepsin B gene shows up regulation and in Alzheimer’s disease down regulation is shown.

Cathepsin B is a very complex protein which is a part of the super family of [http://en.wikipedia.org/wiki/Papain papain-like cystein proteases]. These papain-like cysteine proteases are abundant in nature and can be found in baculovirus, eubacteria, yeast, plants, and animals. They are synthesized as inactive [http://en.wikipedia.org/wiki/Zymogen proenzymes]with N-terminal pro-peptide regions. The pro-peptide plays an important role as an inhibitor of enzymatic activity. A number of cysteine proteases are located within lysosomes and they have very specific functions in endo and exopeptidase activity. Cathepsin B is synthesized as a pre-proenzyme of 339 amino acid residues and it can act as an endopeptidase. Its activity is inhibited by a2-macroglobulin. The most crucial functions of Cathepsin B are that it is implicated in the turnover of proteins and carries out different roles in maintaining the normal metabolism of cells. Cathepsin B is found in humans and other mammals and it is encoded by a single gene and this gene exhibits a high degree of sequence homology to other cysteine proteases of the papain super family. However, in parasitic helmiths and free-living nematodes, the cathepsin B genes can be seen as large multigene families instead of just one single gene shown in humans and mammals. The function of this cathepsin B gene has not been verified for sure, but research is showing that cathepsin B could be involved in induction of protective immunity. In diseases, such as cancer and arthritis, Cathepsin B gene shows up regulation and in Alzheimer’s disease down regulation is shown.

Sandbox Reserved 484: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 18:48, 1 May 2012 view source Alia Raja (talk \| contribs) 74 edits No edit summary ← Older edit		Revision as of 18:50, 1 May 2012 view source Alia Raja (talk \| contribs) 74 edits No edit summary Newer edit →
Line 7:		Line 7:

	[[Image:CTSBFig1.jpg \| thumb]]		[[Image:CTSBFig1.jpg \| thumb]]
	Cathepsin B is a very complex protein which is a part of the super family of [http://en.wikipedia.org/wiki/Papain papain-like cystein proteases]. These papain-like cysteine proteases are abundant in nature and can be found in baculovirus, eubacteria, yeast, plants, and animals. They are synthesized as inactive ~~pro-enzymes~~ with N-terminal pro-peptide regions. The pro-peptide plays an important role as an inhibitor of enzymatic activity. A number of cysteine proteases are located within lysosomes and they have very specific functions in endo and exopeptidase activity. Cathepsin B is synthesized as a pre-proenzyme of 339 amino acid residues and it can act as an endopeptidase. Its activity is inhibited by a2-macroglobulin. The most crucial functions of Cathepsin B are that it is implicated in the turnover of proteins and carries out different roles in maintaining the normal metabolism of cells. Cathepsin B is found in humans and other mammals and it is encoded by a single gene and this gene exhibits a high degree of sequence homology to other cysteine proteases of the papain super family. However, in parasitic helmiths and free-living nematodes, the cathepsin B genes can be seen as large multigene families instead of just one single gene shown in humans and mammals. The function of this cathepsin B gene has not been verified for sure, but research is showing that cathepsin B could be involved in induction of protective immunity. In diseases, such as cancer and arthritis, Cathepsin B gene shows up regulation and in Alzheimer’s disease down regulation is shown.		Cathepsin B is a very complex protein which is a part of the super family of [http://en.wikipedia.org/wiki/Papain papain-like cystein proteases]. These papain-like cysteine proteases are abundant in nature and can be found in baculovirus, eubacteria, yeast, plants, and animals. They are synthesized as inactive [http://en.wikipedia.org/wiki/Zymogen proenzymes]with N-terminal pro-peptide regions. The pro-peptide plays an important role as an inhibitor of enzymatic activity. A number of cysteine proteases are located within lysosomes and they have very specific functions in endo and exopeptidase activity. Cathepsin B is synthesized as a pre-proenzyme of 339 amino acid residues and it can act as an endopeptidase. Its activity is inhibited by a2-macroglobulin. The most crucial functions of Cathepsin B are that it is implicated in the turnover of proteins and carries out different roles in maintaining the normal metabolism of cells. Cathepsin B is found in humans and other mammals and it is encoded by a single gene and this gene exhibits a high degree of sequence homology to other cysteine proteases of the papain super family. However, in parasitic helmiths and free-living nematodes, the cathepsin B genes can be seen as large multigene families instead of just one single gene shown in humans and mammals. The function of this cathepsin B gene has not been verified for sure, but research is showing that cathepsin B could be involved in induction of protective immunity. In diseases, such as cancer and arthritis, Cathepsin B gene shows up regulation and in Alzheimer’s disease down regulation is shown.