Bikunin — not just a plasma proteinase inhibitor

Fries, Erik; Blom, Anna M.

doi:10.1016/s1357-2725(99)00125-9

Cited by 162 publications

(176 citation statements)

References 105 publications

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“…Bikunin is a Kunitz-type protease inhibitor [11] and a structural component of extracellular matrix [12]. Bikunin is the common subunit of a group of protein/carbohydrate complexes that constitute plasma proteins of the inter--inhibitor family [13]. Transcription of the AMBP gene produces an mRNA that is 5 translated into a precursor protein consisting of the A1M and bikunin proteins connected by a linker tripeptide [14].…”

Section: Expressionmentioning

confidence: 99%

A1M, an extravascular tissue cleaning and housekeeping protein

Åkerström¹,

Gram²

2014

Free Radical Biology and Medicine

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Section: Expressionmentioning

confidence: 99%

A1M, an extravascular tissue cleaning and housekeeping protein

Åkerström¹,

Gram²

2014

Free Radical Biology and Medicine

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“…[15][16][17] Bikunin is encoded by an α-microglobulin-bikunin precursor gene, AMBP (Swiss-Prot entry AMBP_HUMAN, P02760). The precursor protein is proteolyzed releasing α-1-microglobulin and bikunin, two proteins with apparently unrelated functions.…”

Section: Introductionmentioning

confidence: 99%

Structural Analysis of Bikunin Glycosaminoglycan

et al. 2008

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The structure of an intact glycosaminoglycan (GAG) chain of the bikunin proteoglycan (PG) was analyzed using a combined top-down and bottom-up sequencing strategy. PGs are proteins with one or more linear, high-molecular weight, sulfated GAG polysaccharides O-linked to serine or threonine residues. GAGs are often responsible for the biological functions of PGs, and subtle variations in the GAG structure have pronounced physiological effects. Bikunin is a serine protease inhibitor found in human amniotic fluid, plasma, and urine. Bikunin is posttranslationally modified with a chondroitin sulfate (CS) chain, O-linked to a serine residue of the core protein.Recent studies have shown that the CS chain of bikunin plays an important role in the physiological and pathological functions of this PG. While no PG or GAG has yet been sequenced, bikunin, the least complex PG, offers a compelling target. Electrospray ionization Fourier transform-ion cyclotron resonance mass spectrometry (ESI FTICR-MS) permitted the identification of several major components in the GAG mixture having molecular masses in a range of 5505-7102 Da. This is the first report of a mass spectrum of an intact GAG component of a PG. FTICR-MS analysis of a size-uniform fraction of bikunin GAG mixture obtained by preparative polyacrylamide gel electrophoresis, allowed the determination of chain length and number of sulfo groups in the intact GAGs.

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“…α 1 m, also known as protein HC [11], is known to be mainly synthesised in the liver, although a minor expression of the protein has been seen in the pancreas and kidney [12,13]. α 1 m is co-expressed with bikunin, a plasma protein with proteinase inhibitor activity and a component of the extracellular matrix [14]. The α 1 mbikunin gene (AMBP) is transcribed and translated into an α 1 m-bikunin precursor protein [15].…”

Section: Introductionmentioning

confidence: 99%