Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0027947 (
neutropenia
)
17,527
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Urinary desmosine excretion (a quantitative measure of endogenous
elastin
breakdown) was monitored in 2 patients with cyclic
neutropenia
. In the first one, measurements were carried out over 2 complete 25-day cycles (nonconsecutive), whereas in the second, measurements were limited to selected urine specimens obtained on days when circulating neutrophils were at undetectable levels. Desmosine excretion remained in the normal range in both patients during neutropenic episodes, suggesting that endogenous
elastin
breakdown was not dependent on neutrophil-mediated elastinolysis. Thus, in alpha 1-antitrypsin-sufficient subjects, any lung
elastin
turnover caused by neutrophils is probably intermittent and limited to times and foci marked by acute inflammatory changes in the lung.
...
PMID:Do neutrophils play a major role in elastin turnover of normal tissues? 685 61
Human granulocyte-macrophage colony-stimulating factor (hGMCSF) is crucial in the immune system as it stimulates survival, proliferation, differentiation, and functional activation of myeloid hematopoietic cells. hGMCSF is integral to approved therapies, including monoclonal antibodies against checkpoint inhibitors, chimeric antigen receptors, and prevention of chemotherapy-induced
neutropenia
. Recombinant hGMCSF can be purified from
Escherichia. coli
; however, it forms inclusion bodies that require solubilization and refolding. Alternatively, this manuscript describes its fusion with an
elastin
-like polypeptide (ELP). Previously reported as purification tags and solubility enhancers, ELPs are recombinant polypeptides that undergo reversible temperature-dependent phase separation. This report is the first to show that fusion to an ELP enables direct purification of hGMCSF fusions from the soluble fraction of bacterial lysate. Surprisingly, these ELP-fusions assemble stable, small, spherical nanoparticles that maintain pro-mitotic activity of hGMCSF. These nanoparticles exhibit ELP-mediated phase separation; however, nanoparticle assembly significantly increases the entropic and enthalpic cost of phase separation compared to ELP alone. The attachment of a high molecular weight ELP to a difficult-to-express protein, like hGMCSF, appears to be a useful strategy to stabilize bioactive, protein-based nanoparticles, which may have broad applications in medicine and biology.
...
PMID:Human Granulocyte-Macrophage Colony-Stimulating Factor Fused to Elastin-Like Polypeptides Assembles Biologically-Active Nanoparticles. 3231 52