Secretory proteins and Balbiani ring gene activities in salivary glands of Chironomus thummi larvae

Chromosoma ◽  
1983 ◽  
Vol 88 (1) ◽  
pp. 16-23 ◽  
Author(s):  
E. Serfling ◽  
L. Meyer ◽  
A. Rudolph ◽  
Kerstin Steiner
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins ◽  
Balbiani Ring ◽  
Chironomus Thummi

Cell-specific synthesis and glycosylation of secretory proteins in larval salivary glands of Chironomus thummi

Chromosoma ◽  
1981 ◽  
Vol 83 (5) ◽  
pp. 661-677 ◽  
Author(s):  
N. N. Kolesnikov ◽  
E. I. Karakin ◽  
Tamara E. Sebeleva ◽  
L. Meyer ◽  
E. Serfling
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins ◽  
Chironomus Thummi ◽  
Specific Synthesis

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

scholarly journals THE ORIENTATION OF DNA WITHIN 80-ANGSTROM CHROMATIN FIBERS

1972 ◽  
Vol 52 (3) ◽  
pp. 639-647 ◽  
Author(s):  
David B. Dusenbery ◽  
Robert B. Uretz
Keyword(s):  
Electron Microscope ◽  
Fluorescence Microscopy ◽  
Salivary Glands ◽  
Acridine Orange ◽  
Average Thickness ◽  
Polarized Fluorescence ◽  
Chromatin Fibers ◽  
The Individual ◽  
Dna Packing ◽  
Chironomus Thummi

Squashing salivary glands of Chironomus thummi larvae, Amblystoma tigrinum erythrocytes, or Spirostromum frequently results in stretched chromatin having highly oriented DNA as determined by polarized fluorescence microscopy of acridine orange-stained preparations. The examination of such material from C. thummi in the electron microscope indicates that the individual chromatin fibers have an average thickness of 80 A as is usually found in embedded and sectioned material. It is thus concluded that the DNA lies nearly parallel to the axis of these chromatin fibers. Detailed calculations of the polarization expected from various models of DNA packing are contained in an appendix.

Induction of balbiani ring puffing changes by sugars and alcohols in Chironomus thummi

1990 ◽  
Vol 20 (5) ◽  
pp. 523-529 ◽  
Author(s):  
Estrella Cortés ◽  
Manuel Serrano ◽  
Rafael J. Yáñez ◽  
JoséL. Díez
Keyword(s):  
Balbiani Ring ◽  
Chironomus Thummi

A tissue-specific puff (Balbiani ring a) in Chironomus thummi may contain a gene encoding a 67-kDa protein which exhibits non-tissue-specific expression

Gene ◽  
1990 ◽  
Vol 96 (2) ◽  
pp. 241-247 ◽  
Author(s):  
S.S. Bogachev ◽  
A.G. Blinov ◽  
N.N. Kolesnikov ◽  
S.V. Scherbik ◽  
A.V. Taranin ◽  
...  
Keyword(s):  
Balbiani Ring ◽  
Gene Encoding ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Chironomus Thummi

scholarly journals Transcriptomic Analysis of Salivary Glands of Ornithodoros brasiliensis Aragão, 1923, the Agent of a Neotropical Tick-Toxicosis Syndrome in Humans

2021 ◽  
Vol 12 ◽  
Author(s):  
Jose Reck ◽  
Anelise Webster ◽  
Bruno Dall’Agnol ◽  
Ronel Pienaar ◽  
Minique H. de Castro ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Secretory Protein ◽  
Clinical Findings ◽  
Host Responses ◽  
Secretory Proteins ◽  
Major Protein ◽  
Host Interaction ◽  
Salivary Gland Protein ◽  
Duplication Events ◽  
Tick Salivary Glands

Tick salivary glands produce and secrete a variety of compounds that modulate host responses and ensure a successful blood meal. Despite great progress made in the identification of ticks salivary compounds in recent years, there is still a paucity of information concerning salivary molecules of Neotropical argasid ticks. Among this group of ticks, considering the number of human cases of parasitism, including severe syndromes and hospitalization, Ornithodoros brasiliensis can be considered one of the major Neotropical argasid species with impact in public health. Here, we describe the transcriptome analysis of O. brasiliensis salivary glands (ObSG). The transcriptome yielded ~14,957 putative contigs. A total of 368 contigs were attributed to secreted proteins (SP), which represent approximately 2.5% of transcripts but ~53% expression coverage transcripts per million. Lipocalins are the major protein family among the most expressed SP, accounting for ~16% of the secretory transcripts and 51% of secretory protein abundance. The most expressed transcript is an ortholog of TSGP4 (tick salivary gland protein 4), a lipocalin first identified in Ornithodoros kalahariensis that functions as a leukotriene C4 scavenger. A total of 55 lipocalin transcripts were identified in ObSG. Other transcripts potentially involved in tick-host interaction included as: basic/acid tail secretory proteins (second most abundant expressed group), serine protease inhibitors (including Kunitz inhibitors), 5' nucleotidases (tick apyrases), phospholipase A2, 7 disulfide bond domain, cystatins, and tick antimicrobial peptides. Another abundant group of proteins in ObSG is metalloproteases. Analysis of these major protein groups suggests that several duplication events after speciation were responsible for the abundance of redundant compounds in tick salivary glands. A full mitochondrial genome could be assembled from the transcriptome data and confirmed the close genetic identity of the tick strain sampled in the current study, to a tick strain previously implicated in tick toxicoses. This study provides novel information on the molecular composition of ObSG, a Brazilian endemic tick associated with several human cases of parasitism. These results could be helpful in the understanding of clinical findings observed in bitten patients, and also, could provide more information on the evolution of Neotropical argasids.

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