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Cleavage of the alp...
Cleavage of the alpha 1-microglobulin-bikunin precursor is localized to the Golgi apparatus of rat liver cells
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- Bratt, Tomas (författare)
- Lund University
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- Olsson, H (författare)
- Lund University
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Sjöberg, E M (författare)
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- Jergil, B (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Akerström, B (författare)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine
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(creator_code:org_t)
- 1993
- 1993
- Engelska.
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Ingår i: Biochimica et Biophysica Acta. - 0006-3002. ; 1157:2, s. 54-147
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- alpha 1-Microglobulin, a plasma protein with immunoregulatory properties, and bikunin, the light chain of the proteinase inhibitors inter-alpha-inhibitor and pre-alpha-inhibitor, are translated as a precursor protein from the same mRNA. The cosynthesis of alpha 1-microglobulin and bikunin is unique compared to other proproteins such as procomplement components and prohormones, since alpha 1-microglobulin and bikunin have no known functional connection. Different forms of intracellular rat liver alpha 1-microglobulin were isolated and characterized by amino acid sequence analysis, lectin binding and glycosidase treatment. Their subcellular distribution was studied by Nycodenz and sucrose gradient centrifugation, pulse-chase experiments, and electrophoresis with subsequent immunoblotting, using pro-C3 and prohaptoglobin as reference proteins. Two alpha 1-microglobulin-bikunin precursors (40 and 42 kDa), containing one and two N-linked oligosaccharides, respectively, were detected in the endoplasmic reticulum. After transport to the Golgi apparatus, the precursors were cleaved, probably C-terminal to the sequence Arg-Ala-Arg-Arg immediately preceding the bikunin part, yielding free sialylated 28 kDa alpha 1-microglobulin, representing the mature protein. The cleavage was almost complete in phosphatidylinositol 4-kinase-enriched membranes, previously identified as a post-Golgi compartment. A fourth intracellular form of alpha 1-microglobulin, 26 kDa, lacked sialic acid. None of the intracellular forms carried the yellow-brown chromophore associated with alpha 1-microglobulin when purified from serum and urine, suggesting that this chromophore becomes linked to the protein after its secretion from the liver cells.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Nyckelord
- 1-Phosphatidylinositol 4-Kinase
- Alpha-Globulins/chemistry
- Animals
- Cells, Cultured
- Glycoproteins/metabolism
- Golgi Apparatus/metabolism
- Liver/metabolism
- Male
- Membrane Glycoproteins
- Phosphotransferases/metabolism
- Protein Precursors/chemistry
- Rats
- Rats, Sprague-Dawley
- Subcellular Fractions/metabolism
- Trypsin Inhibitor, Kunitz Soybean
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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