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

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

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.

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.

scholarly journals Expression of Gross Cystic Disease Fluid Protein-15/Prolactininducible Protein in Rat Salivary Glands

1998 ◽  
Vol 46 (9) ◽  
pp. 1061-1071 ◽  
Author(s):  
Lily Mirels ◽  
Arthur R. Hand ◽  
Holly J. Branin
Keyword(s):  
Salivary Glands ◽  
Acinar Cells ◽  
Secretory Proteins ◽  
Cdna Clones ◽  
Cystic Disease ◽  
Parotid Glands ◽  
Adult Rat ◽  
Rat Salivary Glands ◽  
Inducible Protein ◽  
Cystic Disease Fluid Protein

Gross cystic disease fluid protein-15 (GCDFP-15)/prolactin-inducible protein (PIP) is present at moderate levels in human submandibular and sublingual glands and is barely detectable in human parotid gland. The rodent homologue, PIP, has previously been identified in adult submandibular and lacrimal glands. Here we present the molecular characterization of rat PIP and show that this protein is a product of neonatal and adult rat submandibular, sublingual, and parotid glands. cDNA clones encoding rat PIP were isolated and sequenced. The deduced amino acid sequence of rat PIP shows 56% overall identity and 80% similarity with mouse PIP. By SDS-PAGE, secreted rat PIP has an apparent Mr of 17,000, with a minor proportion present as Mr 20–22,000 N-glycosylated forms. PIP was localized in rat salivary glands by immunogold silver staining. PIP was identified in acinar cells of developing and mature submandibular and parotid glands and at very low levels in sublingual gland serous demilunes. Typically, rat submandibular gland secretory proteins are produced by either acinar cell progenitors (Type III cells) or mature acinar cells. The expression pattern observed for PIP is similar to that previously reported for salivary peroxidase, an important component of nonimmune mucosal defense.

Immunoelectron microscope localization of Mr 90000 heat shock protein and Mr 70000 heat shock cognate protein in the salivary glands of Chironomus thummi

Chromosoma ◽  
1992 ◽  
Vol 102 (1) ◽  
pp. 50-59 ◽  
Author(s):  
G. H. V�zquez-Nin ◽  
O. M. Echeverr�a ◽  
M. E. Carbajal ◽  
R. M. Tanguay ◽  
J. L. Diez ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Salivary Glands ◽  
Heat Shock Cognate Protein ◽  
Chironomus Thummi ◽  
Cognate Protein

Glycosylation of secretory proteins in salivary glands and saliva studied by lectin probes

1996 ◽  
Vol 34 (3) ◽  
pp. 177-180
Author(s):  
J R Garrett ◽  
G B Proctor ◽  
X S Zhang ◽  
D K Shori ◽  
B A Schulte
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins
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