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Citrullination of latency-associated peptide of TGF beta1

ABSTRACT: Enzymatic citrullination of latency-associated peptide of TGF beta1 by PAD2

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Pekka Rappu

LAB HEAD: Jyrki Heino

PROVIDER: PXD003132 | Pride | 2016-03-14

REPOSITORIES: Pride

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			Action	DRS
	150918_PekkaR_LAP_PAD2_inclusion-nr2.mgf	Mgf
	150918_PekkaR_LAP_PAD2_inclusion-nr2.mzid.gz	Mzid
	150918_PekkaR_LAP_PAD2_inclusion-nr2.pride.mgf.gz	Mgf
	150918_PekkaR_LAP_PAD2_inclusion-nr2.pride.mztab.gz	Mztab
	150918_PekkaR_LAP_PAD2_inclusion-nr2.raw	Raw

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Publications

Extracellular citrullination inhibits the function of matrix associated TGF-β.

Sipilä Kalle H KH Ranga Vipin V Rappu Pekka P Torittu Annamari A Pirilä Laura L Käpylä Jarmo J Johnson Mark S MS Larjava Hannu H Heino Jyrki J

Matrix biology : journal of the International Society for Matrix Biology 20160303

In inflammatory arthritis peptidyl arginine deiminase (PAD) enzymes can citrullinate arginine residues in extracellular matrix (ECM) proteins, such as collagens and fibronectin. This may lead to the generation of anti-citrullinated protein antibodies, important diagnostic markers in rheumatoid arthritis. In addition, the citrullination may directly affect protein function. Based on structural analysis, we found that most ECM-associated growth factors (GFs) have arginine residues in their recepto ...[more]

PMID: 26923761

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