Nucleotide sequence of a cDNA encoding rat brain carbonic anhydrase II and its deduced amino acid sequence

Stolle, Catherine A.; McGowan, Michelle H.; Heim, Ruth A.; Varia, Monica; Neubauer, Judith A.

doi:10.1016/0378-1119(91)90619-m

Cited by 16 publications

(5 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Sequencing of the undigested protein proved not to be possible, probably because of N-terminal acylation. However, analyses of Lys-C or trypsin peptide fragments (Ile-Thr-Glu-Ala-Leu-His-Ser-Ile-Lys, Glu-Pro-Ile-Thr-Val-Ser-Ser-Glu-Gln-Met-Ser-His-Phe-Arg-Lys, Ala-Val-Gln-His-Pro-Asp-Gly-Leu-Ala-Val-Leu) were completely identical to the amino acids 158-166, 212-226 and 132-142 of rat brain CAH II (Stolle et al 1991).…”

Section: Identification Of Rat 29-kd Protein As Cah IImentioning

confidence: 83%

“…The purified protein of 29 kD was identified as CAH II using amino acid sequence analyses, immunological studies, and activity assays. The amino acid sequences of three isolated internal peptides revealed 100% identity to CAH II from rat brain (Stolle et al 1991). Furthermore, an anti-coagulating gland CAH II antiserum reacted with the highly homologous human CAH II (Montgomery et al 1987), whereas no immunological crossreactivity to the less related human CAH I and bovine CAH II was detectable (Barlow et al 1987;Sciaky et al 1976).…”

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Wilhelm

Keppler

Hoffbauer

et al. 1998

J Histochem Cytochem.

View full text Add to dashboard Cite

Two different pathways for protein secretion are described for epithelial cells of rat coagulating gland and dorsal prostate: the classical merocrine and the alternative apocrine release mode. Apocrine-secreted proteins are synthesized on cytoplasmic polyribosomes and are subsequently exported in protrusions on the apical cell surface (aposomes). In this article we report the identification and purification to homogeneity of a 29-kD protein from the secretion of rat coagulating gland. N-terminal amino acid sequence analyses revealed 100% identity to rat brain carbonic anhydrase II (CAH II). In addition, the 29-kD protein showed CAH enzyme activity. On Western blot analysis, a polyclonal anti-CAH II antibody raised in rabbit reacted specifically with the rat and human but not bovine CAH II isoforms. Immunohistochemical studies on rat coagulating gland showed strong labeling for CAH II protein in aposomes. Immunoelectron microscopy confined CAH II protein to the cytoplasm and aposomes, whereas no staining was visible in the compartments of the classical merocrine route, the endoplasmic reticulum and Golgi apparatus. The resident cytoplasmic protein lactate dehydrogenase, however, was not found in the secretion. Taken together, the morphological and biochemical data clearly indicate that cytoplasmic CAH II from rat coagulating gland is specifically selected and then secreted via the apocrine pathway.

show abstract

Section: Identification Of Rat 29-kd Protein As Cah IImentioning

confidence: 83%

Section: Discussionmentioning

confidence: 97%

Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Wilhelm

Keppler

Hoffbauer

et al. 1998

J Histochem Cytochem.

View full text Add to dashboard Cite

show abstract

“…Furthermore, there is abundant evidence from individually studied proteins e.g . carbonic anhydrase II from the rat coagulating gland [92], [93], transglutaminase from the prostate [94], [95], an unknown signal peptide lacking protein from the mouse vas deferens (MVDP) [96] that proteins can be released by apocrine mechanism. The reason why specialized individual proteins could appear to be released by apocrine secretion instead of exocytosis is unclear, but one possibility is that they are not individually released at all: the above referenced studies may not have had the tools to examine other components of the secretion and thus their studies were concentrated on a single protein.…”

Section: Discussionmentioning

confidence: 99%

Apocrine Secretion in Drosophila Salivary Glands: Subcellular Origin, Dynamics, and Identification of Secretory Proteins

et al. 2014

View full text Add to dashboard Cite

In contrast to the well defined mechanism of merocrine exocytosis, the mechanism of apocrine secretion, which was first described over 180 years ago, remains relatively uncharacterized. We identified apocrine secretory activity in the late prepupal salivary glands of Drosophila melanogaster just prior to the execution of programmed cell death (PCD). The excellent genetic tools available in Drosophila provide an opportunity to dissect for the first time the molecular and mechanistic aspects of this process. A prerequisite for such an analysis is to have pivotal immunohistochemical, ultrastructural, biochemical and proteomic data that fully characterize the process. Here we present data showing that the Drosophila salivary glands release all kinds of cellular proteins by an apocrine mechanism including cytoskeletal, cytosolic, mitochondrial, nuclear and nucleolar components. Surprisingly, the apocrine release of these proteins displays a temporal pattern with the sequential release of some proteins (e.g. transcription factor BR-C, tumor suppressor p127, cytoskeletal β-tubulin, non-muscle myosin) earlier than others (e.g. filamentous actin, nuclear lamin, mitochondrial pyruvate dehydrogenase). Although the apocrine release of proteins takes place just prior to the execution of an apoptotic program, the nuclear DNA is never released. Western blotting indicates that the secreted proteins remain undegraded in the lumen. Following apocrine secretion, the salivary gland cells remain quite vital, as they retain highly active transcriptional and protein synthetic activity.

show abstract

“…bone, brain, eye, stomach, intestine, liver, pancreas, kidney, red blood cells, salivary glands, and uterus), [34][35][36] and is characterized by its high enzymatic activity and inhibition by exposure to sodium dodecyl sulfate (SDS), owing to the absence of stabilizing disulfide bridges. 7,8,37 As noted above, CAII expression in the nephron accounts for 95% of total CA activity in the kidney, and studies describing the localization of CAII messenger RNA (mRNA) and protein expression in specific nephron segments was recently reviewed in detail.…”

Section: Caiimentioning

confidence: 99%

The role of carbonic anhydrases in renal physiology

Purkerson

Schwartz

2007

Kidney International

205

191

View full text Add to dashboard Cite

Carbonic anhydrase (CA) catalyzes the reversible hydration of CO(2). CA is expressed in most segments of the kidney. CAII and CAIV predominate in human and rabbit kidneys; in rodent kidneys, CAXII, and CAXIV are also present. CAIX is expressed by renal cell carcinoma (RCC). Most of these isoforms, except for rodent CAIV, have high turnover rates. CAII is a cytoplasmic enzyme, whereas the others are membrane-associated; CAIV is anchored by glycosylphosphatidylinositol linkage. Membrane polarity is apical for CAXIV, basolateral for CAXII, and apical and basolateral for CAIV. Luminal membrane CAs facilitate the dehydration of carbonic acid (H(2)CO(3)) that is formed when secreted protons combine with filtered bicarbonate. Basolateral CA enhances the efflux of bicarbonate via dehydration of H(2)CO(3). CAII and CAIV can associate with bicarbonate transporters (e.g., AE1, kNBC1, NBC3, and SCL26A6), and proton antiporter, NHE1 in a membrane protein complex called a transport metabolon. CAXII and CAXIV may also be associated with transporters in normal kidney and CAIX in RCCs. The multiplicity of CAs implicates their importance in acid-base and other solute transport along the nephron. For example, CAII on the cytoplasmic face and CAIV on the extracellular surface provide the 'push' and 'pull' for bicarbonate transport by supplying and dissipating substrate respectively.

show abstract

Nucleotide sequence of a cDNA encoding rat brain carbonic anhydrase II and its deduced amino acid sequence

Cited by 16 publications

References 10 publications

Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Cytoplasmic Carbonic Anhydrase II of Rat Coagulating Gland Is Secreted via the Apocrine Export Mode

Apocrine Secretion in Drosophila Salivary Glands: Subcellular Origin, Dynamics, and Identification of Secretory Proteins

The role of carbonic anhydrases in renal physiology

Contact Info

Product

Resources

About