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Cancer, Cathepsin D is a mitogen and "it attenuates the anti-tumor immune response of decaying chemokines to inhibit the function of dendritic cells". Cathepsins B and L are involved in matrix degradation and cell invasion. [3] Stroke [4] Traumatic brain injury [5] Alzheimer's disease [6] Arthritis [7]
Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. [ 3 ] [ 4 ] [ 5 ] The protein is a cysteine cathepsin , a lysosomal cysteine protease that plays a major role in intracellular protein catabolism .
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
Cathepsin L may refer to: Cathepsin L1 , a human protease enzyme encoded by the CTSL gene and known for its role in viral entry Cathepsin L2 , a human protease enzyme encoded by the CTSV gene and also known as cathepsin V
Several functions of this gene product have now been demonstrated in vitro including membrane-type matrix metalloproteinase inhibition, cathepsin L inhibition, and low-affinity calcium binding. The purified gene product has been shown to inhibit cell attachment and neurite extensions in culture.
The primary function of keratinocytes is the formation of a barrier against environmental damage by heat, UV radiation, dehydration, pathogenic bacteria, fungi, parasites, and viruses.
1515 13039 Ensembl ENSG00000136943 ENSMUSG00000021477 UniProt O60911 P06797 RefSeq (mRNA) NM_001333 NM_001201575 NM_009984 RefSeq (protein) NP_001188504 NP_001324 NP_034114 Location (UCSC) Chr 9: 97.03 – 97.16 Mb Chr 13: 64.51 – 64.52 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in ...
E-64 is an epoxide which can irreversibly inhibit a wide range of cysteine peptidases.. The compound was first isolated and identified from Aspergillus japonicus in 1978. [1] It has since been shown to inhibit many cysteine peptidases such as papain, cathepsin B, cathepsin L, calpain and staphopain.