Severe glomerulonephritis involves cell necrosis as well as NETosis, programmed neutrophil death leading to expulsion of nuclear chromatin and neutrophil extracellular traps (NETs). Histones released by neutrophils undergoing NETosis killed glomerular endothelial cells, podocytes, and parietal epithelial cells. This was prevented by histone-neutralizing agents anti-histone IgG, activated protein C and heparin. Histone toxicity on glomeruli was TLR2/4-dependent. Anti-GBM glomerulonephritis involved NET formation and vascular necrosis. Pre-emptive anti-histone IgG administration significantly reduced all aspects of glomerulonephritis, including vascular necrosis, podocyte loss, albuminuria, cytokine induction, recruitment and activation of glomerular leukocytes and glomerular crescent formation. Subjects with established glomerulonephritis treated with anti-histone IgG, recombinant activated protein C, or heparin all abrogated severe glomerulonephritis suggesting that histone-mediated glomerular pathology is a subsequent, not initial event in necrotizing glomerulonephritis. Neutralizing extracellular histones is therapeutic in severe experimental glomerulonephritis.

Provided herein is technology relating to treatment of sepsis and particularly, but not exclusively, to methods for predicting a response of a sepsis patient to treatment with L-carnitine.

The invention relates to the prevention and treatment of pathologic scars using APC or analogue thereof.

The present application relates to wound repair and wound healing by the application of a therapeutic amount of Activated Protein C-3K3A (APC-3K3A). Specifically, this application is directed to a method of using APC-3K3A for the treatment of dermal or cutaneous wounds, including but not limited to, acute and chronic wounds, burns and ulcers.

The invention provides a polypeptide or a partial polypeptide thereof, containing an amino acid sequence represented by the formula:

A.sub.1A.sub.2A.sub.3(I)

wherein A.sub.1 is an amino acid sequence comprising an amino acid sequence of a light chain of protein C or a homologue thereof, A.sub.2 is an amino acid sequence constituting a self-cleaving site, and A.sub.3 is an amino acid sequence comprising an amino acid sequence of a heavy chain of protein C or a homologue thereof, wherein a dimeric protein or partial protein thereof consisting of fragments on the N-terminal side and C-terminal side of the cleavage site of A.sub.2, has protein C activity. The polypeptide or partial polypeptide thereof makes it possible to 1) produce activated protein C as a recombinant preparation, and 2) link same to effective gene therapy for protein C deficiency.

Compositions and methods useful for the inhibition of cancer metastasis are disclosed.