Hypothalamic cathepsin D: Assay and isoenzyme composition

Akopyan, T. N.; Barchudaryan, N. A.; Karabashyan, L. V.; Arutunyan, A. A.; Lajtha, Ábel; Galoyan, A. A.

doi:10.1002/jnr.490040505

Cited by 8 publications

(3 citation statements)

References 17 publications

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“…Furthermore, prostaglandin F2α and prolactin both function in the rat corpora luteal, with the involvement of cathepsin D [45]. Given the presence of cathepsin D [46], prostaglandin F2α [47], and prolactin [48] in the hypothalamus, an as-yet unknown relationship between the three may exist. All of these differences between PL and ML may affect luteal function and potentially, the transition from the luteal to the follicular phase.…”

Section: Discussionmentioning

confidence: 99%

Comparative Transcriptomics Reveal Key Sheep (Ovis aries) Hypothalamus LncRNAs that Affect Reproduction

Zhang

Tang

et al. 2019

Animals

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The diverse functions of long noncoding RNAs (lncRNAs), which execute their functions mainly through modulating the activities of their target genes, have been have been widely studied for many years (including a number of studies involving lncRNAs in the ovary and uterus). Herein, for the first time, we detect lncRNAs in sheep hypothalami with FecB++ through RNA Sequencing (RNA-Seq) and identify a number of known and novel lncRNAs, with 622 and 809 found to be differentially expressed in polytocous sheep in the follicular phase (PF) vs. monotocous sheep in the follicular phase (MF) and polytocous sheep in the luteal phase (PL) vs. monotocous sheep in the luteal phase (ML), respectively. Then, Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses were performed based on the predicted target genes. The most highly enriched GO terms (at the molecular function level) included carbonyl reductase (NADPH), 15-hydroxyprostaglandin dehydrogenase (NADP+), and prostaglandin-E2 9-reductase activity in PF vs. MF, and phosphatidylinositol-3,5-bisphosphate binding in PL vs. ML was associated with sheep fecundity. Interestingly, the phenomena of valine, leucine, and isoleucine degradation in PL vs. ML, and valine, leucine, and isoleucine biosynthesis in PF vs. MF, were present. In addition, the interactome of lncRNA and its targets showed that MSTRG.26777 and its cis-targets ENSOARG00000013744, ENSOARG00000013700, and ENSOARG00000013777, and MSTRG.105228 and its target WNT7A may participate in the sheep reproductive process at the hypothalamus level. Significantly, MSTRG.95128 and its cis-target Forkhead box L1 (FOXG1) were shown to be upregulated in PF vs. MF but downregulated in PL vs. ML. All of these results may be attributed to discoveries of new candidate genes and pathways related to sheep reproduction, and they may provide new views for understanding sheep reproduction without the effects of the FecB mutation.

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Section: Discussionmentioning

confidence: 99%

Comparative Transcriptomics Reveal Key Sheep (Ovis aries) Hypothalamus LncRNAs that Affect Reproduction

Zhang

Tang

et al. 2019

Animals

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“…All procedures were carried out at 4°C. Endopeptidases activity during purification was assayed at pH 3.2 with pyridoxal-Hb as substrate [18]. A typical enzyme assay was performed in 0.6 ml of reaction mixture, containing 0.05 M citrate buffer, pH 3.2, 100 ,ug of pyridoxal-Hb and various amounts of cathepsin D or HMW aspartic proteinase.…”

Section: Methodsmentioning

confidence: 99%

High molecular weight aspartic endopeptidase generates a coronaro‐constrictory peptide from the β‐chain of hemoglobin

et al. 1993

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Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) aspartic endopeptidase (EC 3.4.23.-) on the processing of hypothalamic calmodulin-binding coronaro-constrictory peptide factors from the p-chain of globin it was found that only HMW aspartic endopeptidase generates the fragment 3140 of the p-chain of bovine hemoglobin (Hb) by cleavage of the Leuso-Leu" and Phe40-Phe41 bonds. Digestion of the B-chain of globin was performed at 37°C at an enzyme/substrate ratio of 1:80 at pH 3.5 using different times of incubation (from 4 h to 10 h). The resulting peptides were separated by reversed-phase high-performance liquid chromatography (HPLC) and then identified by amino acid analysis and Edman degradation. The differences in specificity and activity of these two brain aspartic proteinases could be explained by their different structural features. Our finding provides evidence for a different biological function of these two enzymes. Data obtained give us reason to suppose that HMW aspartic proteinase probably can participate in the processing of the coronaro-constrictory peptide in vivo by limited proteolysis of Hb or Hb-like protein.

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“…a,-Macroglobulin is the only known naturally occurring inhibitor of CD in mammals (Barrett and Starkey, 1973), but other materials in the homogenates of tissue could possibly modify the CD activity measured. CD occurs as three or more isozymes in bovine (Akopyan et al, 1979;Whitaker and Seyer, 1979) and rat (Hackenthal et al, 1 9 7 8~) brain, and it is possible that changes in cell types with selected isozymes or possibly fetal forms of enzymes could account for a discrepancy between measurements of an enzyme protein and enzyme activity. As shown by the present study, CD activity throughout the postnatal period and in the different tissue samples is inhibited by pepstatin.…”

Section: Qqmentioning

confidence: 99%

Postnatal Changes in Cathepsin D in Rat Neural Tissue

Snyder

Whitaker

1983

Journal of Neurochemistry

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Cathepsin D, an aspartyl endopeptidase, was analyzed in cortex from forebrain and cerebellum, spinal cord, and optic and sciatic nerves, and in the liver of rats from 1 to 120 days of age. Cathepsin D was quantitated in tissue extracts by measurement of enzyme specific activity on a substrate of [methyl‐14C]‐methylated hemoglobin and by radioimmunoassay. Immunocytochemistry was used to ascertain the identity of the mixed cell types that contributed to the cathepsin D detected. As quantitated by radioimmunoassay, immunoreactive cathepsin D varied between 0.2 and 1 ng/μg of total protein. Maximum activity occurred at approximately the 15th postnatal day; the least amount of immunoreactive cathepsin D was found at 30 or 60 days of age. A subsequent increase of varying magnitude occurred at postnatal day 120. There was good correspondence between immunoreactive enzyme and enzyme specific activity, which ranged from 1 to 4 ng/μg of total protein, and the activities determined by the two methods provided similar, but not identical, developmental profiles. Cathepsin D was demonstrated by immunocytochemistry to be present in most neurons, in all choroid plexus epithelium, and in certain oligodendrocytes from the first postnatal day. Cathepsin D was present in oligodendrocytes in cord lateral funiculi and optic nerve by the first postnatal day, and by the sixth postnatal day many oligodendrocytes were abundantly stained. In contrast, oligodendrocytes in the corpus callosum and in the cerebellar white matter did not contain demonstrable cathepsin D until postnatal days 10 and 15, respectively. These results indicate a role for cathepsin D during the postnatal development of rat CNS and suggest that this proteinase may be involved in the steps of myelination.

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Hypothalamic cathepsin D: Assay and isoenzyme composition

Cited by 8 publications

References 17 publications

Comparative Transcriptomics Reveal Key Sheep (Ovis aries) Hypothalamus LncRNAs that Affect Reproduction

Comparative Transcriptomics Reveal Key Sheep (Ovis aries) Hypothalamus LncRNAs that Affect Reproduction

High molecular weight aspartic endopeptidase generates a coronaro‐constrictory peptide from the β‐chain of hemoglobin

Postnatal Changes in Cathepsin D in Rat Neural Tissue

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