منابع مشابه
ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family.
We report the primary structure of three novel, putative zinc metalloproteases designated ADAM-TS5, ADAM-TS6, and ADAM-TS7. All have a similar domain organization, comprising a preproregion, a reprolysin-type catalytic domain, a disintegrin-like domain, a thrombospondin type-1 (TS) module, a cysteine-rich domain, a spacer domain without cysteine residues, and a COOH-terminal TS module. These ge...
متن کاملADAM-family metalloproteinases in lung inflammation: potential therapeutic targets.
Acute and chronic lung inflammation is driven and controlled by several endogenous mediators that undergo proteolytic conversion from surface-expressed proteins to soluble variants by a disintegrin and metalloproteinase (ADAM)-family members. TNF and epidermal growth factor receptor ligands are just some of the many substrates by which these proteases regulate inflammatory or regenerative proce...
متن کاملRole for ADAM-family proteinases as membrane protein secretases.
Introduction Over 10 years ago, while studying the topology and mode of anchorage of angiotensin-converting enzyme (ACE) in brush border membranes of pig kidney, we observed that a substantial portion of the ACE activity was released in a tirnedependent manner into the soluble supernatant fraction after centrifugation [ 11. This solubilized ACE activity was hydrophilic and could not reconstitut...
متن کاملShedding of membrane proteins by ADAM family proteases.
Many membrane-bound proteins undergo proteolytic release from the membrane, a process known as 'shedding'. Some of the processing events are carried out by enzymes of the ADAM (a disintegrin and metalloproteinase) family, which are also membrane bound. One of the most well known ADAM family members is TACE (tumour necrosis factor-alpha-converting enzyme. TACE was the first ADAM family member to...
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ژورنال
عنوان ژورنال: Fly
سال: 2012
ISSN: 1933-6934,1933-6942
DOI: 10.4161/fly.18823