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Biomedical subjects

Teruo Ichikawa

Publications and source records attributed to Teruo Ichikawa.

4 recordsLinked to original sources
PubMed2006

Endodermal cyst ventral to the lower brain stem.

A 28-year-old woman presented with a rare case of endodermal cyst located ventral to the lower brain stem manifesting as recurrent aseptic meningitis. Computed tomography and magnetic resonance imaging demonstrated a cystic mass located ventral to the lower brain stem and extending from the prepontine to the upper cervical (C-2) cistern. The lesion was totally removed through a retrosigmoid craniotomy and C1-2 hemilaminectomy. Histological and immunohistochemical examination showed the cyst was derived from the endoderm. The histological diagnosis was endodermal cyst. Early diagnosis and surgical removal are important for patients with these cysts.

Adult↗
PubMed2003

SNA-60-367 components, new peptide enzyme inhibitors of aromatase: structure of the fatty acid side chain and amino acid sequence by mass spectrometry.

SNA-60-367 components, new peptide enzyme inhibitors of aromatase, were isolated from the culture broth of soil bacterium, Bacillus sp. SNA-60-367. These inhibitors are a family of acylated decapeptides that differ from each other in terms of amino acid composition and the nature of the fatty acid side chain. The structures of the fatty acid moieties were shown to be (3-hydroxy)heptadecanoic acid and (3-hydroxy)hexadecanoic acid that possess normal-, iso- or anteiso-type alkyl groups. The amino acid sequence of the open form of the lactone ring of the acylpeptides is RCO-L-Glu-D-Orn-L(or D)-Tyr3-D-allo-Thr-L-Glu-D-X1 (Ala, Aba or Val)-L-Pro-L-Gln-D(or L)-Tyr-L-X2(10)(Ile or Val)-OH. The lactone ring of SNA-60-367 components is formed between Tyr3 and X2(10).

Aromatase Inhibitors↗
PubMed2002

Propeptin, a new inhibitor of prolyl endopeptidase produced by microbispora II. Determination of chemical structure.

The structure of propeptin, a new inhibitor of prolyl endopeptidase isolated from Microbispora sp. SNA-115, was determined. FAB/MS, Edman degradation and amino acid analysis revealed propeptin to be a cyclic polypeptide consisting of 19 common L-amino acids. By FAB/MS and protein chemical methods, the primary sequence of propeptin was determined to be Gly1-Tyr-Pro-Trp-Trp-Asp-Tyr-Arg-Asp9-Leu-Phe-Gly-Gly-His-Thr-Phe-Ile-Ser-Pro19, which cyclizes between the beta-carboxyl group of Asp9 and the a-amino group of Gly1.

Actinomycetales↗