{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,27]],"date-time":"2025-11-27T06:24:45Z","timestamp":1764224685299},"reference-count":46,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2002,7,11]],"date-time":"2002-07-11T00:00:00Z","timestamp":1026345600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Arch Insect Biochem Physiol"],"published-print":{"date-parts":[[2002,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We isolated and sequenced cDNA clones corresponding to two storage proteins (HcSP\u20101 and HcSP\u20102) from fall webworm,<jats:italic>Hyphantria cunea<\/jats:italic>. The cDNAs for HcSP\u20101 (2,337 bp) and HcSP\u20102 (2,572 bp) code for 753 and 747 residue proteins with predicted molecular masses of 88.3 and 88.5 kDa, respectively. The calculated isoelectric points are pI = 8.4 (HcSP\u20101) and 7.6 (HcSP\u20102). Multiple alignment analysis of the amino acid sequence revealed that HcSP\u20101 is most similar to SL\u20101 from<jats:italic>S. litura<\/jats:italic>(73.8% identity) and other methionine\u2010rich hexamers, whereas HcSP\u20102 is most similar to the SL\u20102 \u03b1 subunit from<jats:italic>S. litura<\/jats:italic>(74.8% identity) and other moderately methionine\u2010rich hexamers. The two storage proteins from<jats:italic>H. cunea<\/jats:italic>shared only 38.4% identity with one another. According to both phylogenetic analyses and the criteria of amino acid composition, HcSP\u20101 belongs to the subfamily of Met\u2010rich storage proteins (6% methionine, 10% aromatic amino acid), and HcSP\u20102 belongs to the subfamily of moderately methionine\u2010rich storage proteins (3.2% methionine, 12.9% aromatic amino acid). Topical application of the JH analog, methoprene, after head ligation of larvae, suppressed transcription of the SP genes, indicating hormonal effects at the transcriptional level. The HcSP\u20101 transcript was detected by Northern blot analysis in Malpighian tubule, testis, and ovary, in addition to fat body where it was most abundant. The HcSP\u20102 transcript was detected only in fat body and Malpighian tubule. The accumulation of HcSP\u20101 in ovary and HcSP\u20102 in Malpighian tubule might be related to differential functions in both organs. Arch. Insect Biochem. Physiol. 50:157\u2013172, 2002. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/arch.10040","type":"journal-article","created":{"date-parts":[[2002,10,6]],"date-time":"2002-10-06T11:46:55Z","timestamp":1033904815000},"page":"157-172","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Two juvenile hormone suppressible storage proteins may play different roles in<i>Hyphantria cunea<\/i>Drury"],"prefix":"10.1002","volume":"50","author":[{"given":"Hyang\u2010Mi","family":"Cheon","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Su\u2010Jeong","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hong\u2010Ja","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Byung 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