Linked Life Data

11278730

Source:http://linkedlifedata.com/resource/pubmed/id/11278730

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2001-6-11
pubmed:abstractText
A group of 16-kDa proteins, synthesized and secreted by rat pancreatic acinar cells and composed of pancreatic stone protein (PSP/reg) and isoforms of pancreatitis-associated protein (PAP), show structural homologies, including conserved amino acid sequences, cysteine residues, and highly sensitive N-terminal trypsin cleavage sites, as well as conserved functional responses in conditions of pancreatic stress. Trypsin activation of recombinant stress proteins or counterparts contained in rat pancreatic juice (PSP/reg, PAP I and PAP III) resulted in conversion of 16-kDa soluble proteins into 14-kDa soluble isoforms (pancreatic thread protein and pancreatitis-associated thread protein, respectively) that rapidly polymerize into insoluble sedimenting structures. Activated thread proteins show long lived resistance to a wide spectrum of proteases contained in pancreatic juice, including serine proteases and metalloproteinases. In contrast, PAP II, following activation with trypsin or pancreatic juice, does not form insoluble structures and is rapidly digested by pancreatic proteases. Scanning and transmission electron microscopy indicate that activated thread proteins polymerize into highly organized fibrillar structures with helical configurations. Through bundling, branching, and extension processes, these fibrillar structures form dense matrices that span large topological surfaces. These findings suggest that PSP/reg and PAP I and III isoforms consist of a family of highly regulated soluble secretory stress proteins, which, upon trypsin activation, convert into a family of insoluble helical thread proteins. Dense extracellular matrices, composed of helical thread proteins organized into higher ordered matrix structures, may serve physiological functions within luminal compartments in the exocrine pancreas.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21028-38
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11278730-Amino Acid Sequence, pubmed-meshheading:11278730-Animals, pubmed-meshheading:11278730-Calcium-Binding Proteins, pubmed-meshheading:11278730-Cloning, Molecular, pubmed-meshheading:11278730-Genetic Vectors, pubmed-meshheading:11278730-Heat-Shock Proteins, pubmed-meshheading:11278730-Kinetics, pubmed-meshheading:11278730-Lithostathine, pubmed-meshheading:11278730-Microscopy, Electron, pubmed-meshheading:11278730-Molecular Sequence Data, pubmed-meshheading:11278730-Nerve Tissue Proteins, pubmed-meshheading:11278730-Pancreas, pubmed-meshheading:11278730-Peptide Fragments, pubmed-meshheading:11278730-Phosphoproteins, pubmed-meshheading:11278730-Pichia, pubmed-meshheading:11278730-Protein Isoforms, pubmed-meshheading:11278730-Rats, pubmed-meshheading:11278730-Recombinant Proteins, pubmed-meshheading:11278730-Sequence Alignment, pubmed-meshheading:11278730-Trypsin
pubmed:year
2001
pubmed:articleTitle
A family of 16-kDa pancreatic secretory stress proteins form highly organized fibrillar structures upon tryptic activation.
pubmed:affiliation
Pancreatitis Research Laboratory, Department of Visceral Surgery, University Hospital, Zürich, 8091, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't