Association of Matrix Metalloproteinases -7, -8 and -9 and TIMP -1 with Disease Severity in Acute Pancreatitis. A Cohort Study
PLoS ONE, 2016;11(8):e0161480.
Species: Human
Sample Type: Plasma

In vitro progesterone modulation on bacterial endotoxin-induced production of IL-1beta, TNFalpha, IL-6, IL-8, IL-10, MIP-1alpha, and MMP-9 in pre-labor human term placenta.
Authors: Garcia-Ruiz G, Flores-Espinosa P, Preciado-Martinez E, Bermejo-Martinez L, Espejel-Nunez A, Estrada-Gutierrez G, Maida-Claros R, Flores-Pliego A, Zaga-Clavellina V
Reprod Biol Endocrinol, 2015;13(0):115.
Species: Human
Sample Type: Cell Culture Supernates

Serum metalloproteinase-9 is related to COPD severity and symptoms - cross-sectional data from a population based cohort-study.
Authors: Linder R, Ronmark E, Pourazar J, Behndig A, Blomberg A, Lindberg A
Respir Res, 2015;16(0):28.
Species: Human
Sample Type: Serum

Therapy with plasma purified alpha1-antitrypsin (Prolastin(R)) induces time-dependent changes in plasma levels of MMP-9 and MPO.
Authors: Koepke J, Dresel M, Schmid S, Greulich T, Beutel B, Schmeck B, Vogelmeier C, Janciauskiene S, Koczulla A
PLoS ONE, 2015;10(0):.
Species: Human
Sample Type: Serum

Recognition of bacterial signal peptides by mammalian formyl peptide receptors: a new mechanism for sensing pathogens.
Authors: Bufe B, Schumann T, Kappl R, Bogeski I, Kummerow C, Podgorska M, Smola S, Hoth M, Zufall F
J Biol Chem, 2015;290(12):7369-87.
Species: Human
Sample Type: Cell Culture Supernates

Compartment differences of inflammatory activity in chronic obstructive pulmonary disease.
Authors: Ji J, von Scheele I, Bergstrom J, Billing B, Dahlen B, Lantz A, Larsson K, Palmberg L
Respir Res, 2014;15(0):104.
Species: Human
Sample Type: Serum

Identification of neutrophil activation markers as novel surrogate markers of CF lung disease.
Authors: Rath T, Zwaschka L, Hage L, Kugler M, Menendez K, Naehrlich L, Schulz R, Roderfeld M, Roeb E
PLoS ONE, 2014;9(12):e115847.
Species: Human
Sample Type: Serum

Clinical utility of diagnostic guidelines and putative biomarkers in lymphangioleiomyomatosis.
Respir. Res., 2012;13(0):34.
Species: Human
Sample Type: Serum

Non-acylated Mycobacterium bovis glycoprotein MPB83 binds to TLR1/2 and stimulates production of matrix metalloproteinase 9.
Authors: Chambers MA, Whelan AO, Spallek R
Biochem. Biophys. Res. Commun., 2010;400(3):403-8.
Species: Human
Sample Type: Cell Culture Supernates

Interferon-gamma reverses the immunosuppressive and protumoral properties and prevents the generation of human tumor-associated macrophages.
Authors: Duluc D, Corvaisier M, Blanchard S, Catala L, Descamps P, Gamelin E, Ponsoda S, Delneste Y, Hebbar M, Jeannin P
Int. J. Cancer, 2009;125(2):367-73.
Species: Human
Sample Type: Cell Culture Supernates

Cerebrospinal fluid B cells correlate with early brain inflammation in multiple sclerosis.
Authors: Kuenz B, Lutterotti A, Ehling R, Gneiss C, Haemmerle M, Rainer C, Deisenhammer F, Schocke M, Berger T, Reindl M
PLoS ONE, 2008;3(7):e2559.
Species: Human
Sample Type: Serum

Matrix metalloproteinases and their tissue inhibitors (TIMPs) in Plasmodium falciparum malaria: serum levels of TIMP-1 are associated with disease severity.
Authors: Dietmann A, Helbok R, Lackner P, Issifou S, Lell B, Matsiegui PB, Reindl M, Schmutzhard E, Kremsner PG
J. Infect. Dis., 2008;197(11):1614-20.
Species: Human
Sample Type: Serum

Association of matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-4 in cerebrospinal fluid with blood-brain barrier dysfunction in patients with eosinophilic meningitis caused by Angiostrongylus cantonensis.
Authors: Tsai HC, Chung LY, Chen ER, Sy CL
Am. J. Trop. Med. Hyg., 2008;78(1):20-7.
Species: Human
Sample Type: CSF

The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP).