Biomedical subjects

J Biber

Publications and source records attributed to J Biber.

At least 145 records · Page 8Linked to original sources

PubMed1994

Electrogenic cotransport of Na+ and sulfate in Xenopus oocytes expressing the cloned Na+SO4(2-) transport protein NaSi-1.

The Na+/sulfate cotransporter cloned from rat kidney cortex (NaSi-1) has been expressed in oocytes of Xenopus laevis and subjected to electrophysiological analysis by current and voltage clamp methods. In current-clamped oocytes, superfusion with 1 mM sulfate resulted in a 12-mV depolarization of the cell membrane. Accordingly, in voltage-clamped oocytes sulfate induced an inward current IS, which was dependent on both the concentration of Na+ and sulfate in the superfusate. Half-maximal IS was observed at about 0.1 mM sulfate and 70 mM Na+. The Hill coefficients were 1 and 2.8 for sulfate and Na+, respectively. Thiosulfate and selenate created similar currents as sulfate with a similar Km. At saturating concentrations of thiosulfate and selenate, addition of sulfate could not induce an additive current. Phosphate (1 mM) did not inhibit sulfate-induced currents. Finally, IS was dependent on the holding potential being larger at more negative potentials. The results of this study strongly suggest an electrogenic cotransport of sulfate and Na+ with a stoichiometry of 1:3.

Animals↗

PubMed1994

Cloning of a Na/Pi cotransporter from opossum kidney cells.

Opossum kidney (OK) cells have been extensively used to study cellular mechanisms of renal proximal tubular Na/P(i) cotransport. We have cloned a cDNA (NaPi-4) most likely encoding an apical Na/P(i) cotransporter from OK cells. The cloning strategy was based on homology to the recently cloned human renal (NaPi-3) Na/P(i) cotransporter (Magagnin, S., Werner, A., Markovich, D., Sorribas, V., Stange, G., Biber, J., and Murer, H. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 5979-5983). Kinetic characterization (P(i) interaction, sodium interaction, and pH dependence) of NaPi-4-induced Na/P(i) uptake showed high similarity to apical Pi transport in OK cell monolayers. The NaPi-4 cDNA is 2548 base pairs long and encodes a protein of 70.5 kDa, containing at least 8 predicted transmembrane domains. Northern blot analysis with OK cell mRNA shows a NaPi-4-related signal (2.5 kilobases) in cells grown on impermeant and permeant supports. Hybrid depletion with NaPi-4 antisense oligonucleotides abolished the mRNA-induced Na/P(i) cotransport in oocytes. Similarly, NaPi-4 antisense oligonucleotides inhibited (up to 70%) Na/P(i) cotransport in OK cell monolayers. We presume that NaPi-4 is closely related to the OK cell apical Na/P(i) cotransporter.

Amino Acid Sequence↗

PubMed1994

Increase of Na/Pi-cotransport encoding mRNA in response to low Pi diet in rat kidney cortex.

Renal proximal Na/Pi-cotransport is increased in response to low dietary Pi intake. Recently, a cDNA (NaPi-2) related to the rat renal brush membrane Na/Pi-cotransporter has been cloned. In the present study, we used rats fed for 6 days with either a low Pi diet (LPD) or a high Pi diet (HPD), respectively. In parallel to an increased renal brush-border membrane Na/Pi-cotransport in LPD rats, there was also an increased content of NaPi-2 mRNA in renal cortex. After injection into Xenopus laevis oocytes, mRNA isolated from LPD rats induced a greater increase in Na/Pi-cotransport compared to mRNA from HPD rats. Hybrid depletion experiments suggested that mRNA-induced Na/Pi-cotransport is related to NaPi-2. We conclude that chronic Pi deprivation leads to an increased brush-border membrane Na/Pi-cotransport via an increase in the level of (NaPi-2) mRNA.

Animals↗

PubMed1994

Nephron localization of Na/SO4(2-)-cotransport-related mRNA and protein.

A Na+/SO4(2-)-cotransport system was recently identified from a rat kidney cortex cDNA library by expression cloning (NaSi-1;). In this work the sites of expression of NaSi-1-related mRNA and protein were determined using reverse transcriptase-polymerase chain reaction (RT-PCR) with microdissected nephron segments, and Western blot analysis on isolated tubules or purified membranes using polyclonal antibodies against the C-terminus of NaSi-1. Expression of both NaSi-1-related mRNA and protein was observed in proximal tubules and in papillary collecting ducts. Membrane separation studies indicated that in proximal tubules the NaSi-1-related protein is expressed apically. The observed distribution patterns (together with the earlier functional analysis) of NaSi-1-related mRNA and protein suggest that the NaSi-1 protein is involved in proximal tubular brush-border membrane Na+/SO4(2-)-cotransport. The functional correlation of the observed expression of the NaSi-1-related protein in collecting ducts remains to be determined.

Animals↗

PubMed1994

Expression of a renal Na(+)-nucleoside cotransport system (N2) in Xenopus laevis oocytes.

Xenopus laevis oocytes have been used for the expression of a renal, pyrimidine-selective, Na(+)-nucleoside cotransporter (N2). As compared to its uptake in water-injected oocytes, Na(+)-dependent thymidine uptake was enhanced in a time- and dose-dependent manner in oocytes injected with rat renal cortex total poly(A)+ RNA. An increased uptake was also observed after injection of size fractionated rat renal cortex poly(A)+ RNA (2-3 kb). Consistent with the selectivity of the N2 nucleoside transporter, cytidine significantly inhibited Na(+)-dependent thymidine uptake in oocytes injected with total poly(A)+ RNA whereas guanosine and formycin B did not. Na(+)-dependent thymidine uptake was also enhanced in oocytes injected with size fractionated human renal cortex poly(A)+ RNA (2-3 kb). The above data demonstrate functional expression of renal cortex, Na(+)-nucleoside cotransporters in Xenopus laevis oocytes.

Animals↗

PubMed1994

Low-Pi diet increases the abundance of an apical protein in rat proximal-tubular S3 segments.

Dietary phosphate (Pi) restriction is associated with an adaptive increase in proximal-tubular apical brush-border membrane (BBM) sodium-dependent Pi transport (Na-Pi cotransport). Adaptation to Pi restriction is dependent on de novo protein synthesis; however, it is not known whether the proteins involved represent newly synthesized Na-Pi cotransporters or some other (regulatory) proteins. Recently the cDNA for a Na-Pi cotransport system of rabbit kidney cortex (system NaPi-1) has been identified by expression cloning. The purpose of this study was to determine if the adaptive increase in Na-Pi cotransport in response to dietary Pi restriction in the rat is associated with an increase in the abundance of a NaPi-1-related protein. To answer this question we took advantage of the cross-reactivity of polyclonal antibodies raised against a C-terminal peptide of the NaPi-1 protein with a protein of BBM isolated from rat kidney cortex. On Western blots, a positive reaction with a protein with an apparent molecular mass of 100 kDa was observed in BBM isolated from juxtamedullary cortex and, to a lesser extent, in BBM isolated from superficial cortex. In immunohistochemical studies anti-(NaPi-1)-antiserum-mediated immunofluorescence was observed predominantly in S3 segments where the immunoreaction was restricted to the brush borders. Compared to control BBM, in BBM isolated from the juxtamedullary cortex of rats fed a low-Pi diet, there was a twofold increase in the abundance of the 100-kDa protein. In the same membrane vesicles Na-Pi cotransport was increased threefold. The results of this study demonstrate specific expression of a 100-kDa apical protein in S3 cells of rat proximal tubules. Increased abundance of the 100-kDa protein due to chronic Pi restriction suggests an involvement of this protein in the (chronic) adaptive response of S3 cells to a low-Pi diet.

Adaptation, Physiological↗

PubMed1994

Renal sodium-phosphate cotransport.

Proximal tubular reabsorption of inorganic phosphate (P(i) is a major determinant of the extracellular concentration of phosphate. The net proximal reabsorption of phosphate largely depends on the rate of apical sodium-dependent transport of P(i) (Na/P(i) cotransport), which is controlled by various hormonal and nonhormonal factors. Renal Na/P(i) cotransport systems that represent proximal apical Na/P(i) cotransport systems have recently been identified. Molecular knowledge of proximal tubular Na/P(i) cotransport will lead to a new understanding of the cellular mechanisms of the physiologic control of proximal P(i) reabsorption and to elucidation of the pathophysiologic mechanisms impairing P(i) homeostasis.

Animals↗

PubMed1994

Metabolism and transport of the pentapeptide metkephamid by brush-border membrane vesicles of rat intestine.

Intestinal metabolism and transport of the pentapeptide metkephamid (Tyr-D-Ala-Gly-Phe-N-Me-Met-NH2) were studied using isolated brush-border membranes from the rat. Analysis of the metabolic fragments of enzymatic hydrolysis revealed that cleavage of the N-terminal peptide bond leads to the formation of tyrosine and a tetrapeptide D-Ala-Gly-Phe-N-Me-Met-NH2. The inactivation was due to aminopeptidase N activity and could be inhibited by peptidase inhibitors puromycin, bacitracin and certain dipeptides. Transport studies demonstrated uptake of the intact pentapeptide into the intravesicular space of the vesicles. The transport was a first-order process; no participation of known intestinal peptide carrier systems in the transport of metkephamid could be shown. Modelling of simultaneous metabolism and transport kinetics suggests strategies to improve the fraction absorbed of a peptide by either decreasing its affinity to the metabolizing enzymes (increase Km) or decreasing the concentration of the metabolizing enzymes e.g. by delivering the peptide to an absorption site with reduced enzymatic activity (decrease Vmax) or increasing its absorption velocity.

Amino Acid Sequence↗

PubMed1994

Expression of Na-P(i) cotransport in rat kidney: localization by RT-PCR and immunohistochemistry.

We have recently identified a rat kidney cortex Na-dependent transport system for phosphate (P(i)) by expression cloning (NaP(i)-2) (S. Magagnin, A. Werner, D. Markovich, V. Sorribas, G. Stange, J. Biber, and H. Murer. Proc. Natl. Acad. Sci. USA 90: 5979, 1993). In this study we have used reverse transcription-polymerase chain reaction (RT-PCR) and immunohistochemistry to establish the sites of expression of the NaP(i)-2-related mRNA and protein. RT-PCR was performed with single microdissected nephron segments. From these experiments we conclude that NaP(i)-2 mRNA is predominantly expressed in the proximal tubules of superficial and deep nephrons. No NaP(i)-2 mRNA was detected in the thick ascending limb of Henle's loop; however, faint NaP(i)-2 related PCR products were also observed in collecting ducts. Expression of the NaP(i)-2 protein was examined with the use of polyclonal antibodies raised against synthetic NaP(i)-2-derived peptides. Strong specific anti-NaP(i)-2 antiserum-mediated immunofluorescence was found in the convoluted part of proximal tubules and gradually decreased along the straight part. Immunofluorescence indicated that the NaP(i)-2 protein is present in the brush border of proximal tubular cells. In addition, NaP(i)-2-specific immunofluorescence was also observed in subapical vesicles. The described distribution of the NaP(i)-2 protein is in agreement with previously described nephron sites of P(i) reabsorption in the rat kidney and therefore suggests that the NaP(i)-2 transport system represents an Na-P(i) cotransporter involved in proximal tubular apical transport of phosphate.

Animals↗

PubMed1994

Cellular mechanisms of acute and chronic adaptation of rat renal P(i) transporter to alterations in dietary P(i).

Recently, the cDNA for a Na-P(i) cotransport system of rat kidney cortex (NaPi-2) has been identified by expression cloning. Using polyclonal antibodies raised against this renal Na-P(i) cotransport system, and using the polymerase chain reaction after reverse transcription of mRNA in microdissected nephron segments, we recently demonstrated that NaPi-2-related mRNA and protein is expressed in the brush-border membranes (BBM) of the proximal tubules of rat kidney. The purpose of the present study was to study the cellular mechanisms involved in adaptation of rat renal Na-P(i) cotransporter to acute and chronic alterations in dietary P(i). Compared with rats fed chronically (7 days) a high-P(i) diet (1.2%), in rats fed chronically a low-P(i) (0.1%) diet the 3.4-fold increase in BBM Na-P(i) cotransport rate (chronic upregulation) was associated with a 2.2-fold increase in renal cortical NaPi-2 mRNA and a 4.9-fold increase in BBM NaPi-2 protein abundances. In contrast, compared with rats fed chronically (7 day) a high-P(i) diet, in rats fed acutely (2 h) a low-P(i) diet the 1.5-fold increase in Na-P(i) cotransport rate (acute upregulation) was associated with a 1.8-fold increase in NaPi-2 protein but no change in NaPi-2 mRNA abundance. Similarly, compared with rats fed chronically a low-P(i) diet, in rats fed acutely (2 h) a high-P(i) diet the 1.9-fold decrease in Na-P(i) cotransport rate (acute downregulation) was associated with a 3.8-fold decrease in NaPi-2 protein but no change in NaPi-2 mRNA abundance.(ABSTRACT TRUNCATED AT 250 WORDS)

Acclimatization↗

PubMed1994

Renal Na(+)-phosphate cotransport in murine X-linked hypophosphatemic rickets. Molecular characterization.

The X-linked Hyp mouse is characterized by a specific defect in proximal tubular phosphate (Pi) reabsorption that is associated with a decrease in Vmax of the high affinity Na(+)-Pi cotransport system in the renal brush border membrane. To understand the mechanism for Vmax reduction, we examined the effect of the Hyp mutation on renal expression of Na(+)-Pi cotransporter mRNA and protein. Northern hybridization of renal RNA with a rat, renal-specific Na(+)-Pi cotransporter cDNA probe (NaPi-2) (Magagnin et al. 1993. Proc. Natl. Acad. Sci. USA. 90:5979-5983.) demonstrated a reduction in a 2.6-kb transcript in kidneys of Hyp mice relative to normal littermates (NaPi-2/beta-actin mRNA = 57 +/- 6% of normal in Hyp mice, n = 6, P < 0.01). Na(+)-Pi cotransport, but not Na(+)-sulfate cotransport, was approximately 50% lower in Xenopus oocytes injected with renal mRNA extracted from Hyp mice when compared with that from normal mice. Hybrid depletion experiments documented that the mRNA-dependent expression of Na(+)-Pi cotransport in oocytes was related to NaPi-2. Western analysis demonstrated that NaPi-2 protein is also significantly reduced in brush border membranes of Hyp mice when compared to normals. The present data demonstrate that the specific reduction in renal Na(+)-Pi cotransport in brush border membranes of Hyp mice can be ascribed to a proportionate decrease in the abundance of Na(+)-Pi cotransporter mRNA and protein.

Animals↗

PubMed1994

Apical and basolateral parathyroid hormone receptors in rat renal cortical membranes.

Brush border (BBM) and basolateral membranes (BLM) of rat renal cortical cells separated by free flow electrophoresis revealed two distinct peaks of BBM-specific leucine aminopeptidase and Na+/K(+)-ATPase for BLM. PTH/PTH-related protein (PTHrP) receptors were identified in BBM and BLM. Specific binding of 125 pM [125I]chicken [Tyr36]-PTHrP-(1-36)amide [chPTHrP-(1-36)] to individual fractions of membranes separated by free flow electrophoresis overlapped with the leucine aminopeptidase and Na+/K(+)-ATPase profiles. Binding to pooled BBM was 53 +/- 5% (mean +/- SEM) of that to BLM (P < 0.01). In BBM and BLM, half-maximal inhibition of binding was obtained with 0.4-0.9 nM chPTHrP-(1-36) and 0.2-0.6 nM rat PTH-(1-34). Guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S; 100 microM) lowered chPTHrP-(1-36) binding to 50% of control levels, and half-maximal inhibition of binding was obtained with 480 and 8 nM GTP gamma S in BBM and BLM, respectively. Cross-linking of the PTH/PTHrP receptors with [125I]chPTHrP-(1-36) modified with N-hydroxysuccinimidyl-4-azidobenzoate revealed indistinguishable doublets of 83 and 73 kilodaltons in both BBM and BLM. Adenylyl cyclase was stimulated 6- and 10-fold by chPTHrP-(1-36) and GTP gamma S, respectively, in BLM and 1.3- and 1.9-fold in BBM. In conclusion, PTH receptors were recognized in both the basolateral and brush border membranes. Different receptor coupling to G-proteins and minimal cAMP stimulation in BBM provide evidence for PTH/PTHrP receptor isotypes and/or different postreceptor activation in BBM and BLM.

Adenylyl Cyclases↗

PubMed1994

Renal and small intestinal sodium-dependent symporters of phosphate and sulphate.

Homeostasis of inorganic phosphate (P(i)) and sulphate (Si) is largely achieved by absorption in the mammalian small intestine and by reabsorption in the proximal tubule of the kidney. Under normal physiological conditions, the kidney appears to play the major role in maintaining the extracellular concentration of these anions. In both epithelia, reabsorption of P(i) and to some extent also of Si underlie a variety of regulatory acute and chronic control mechanisms. Acute regulatory mechanisms are predominantly found in renal P(i) reabsorption, whereas chronic regulation of transepithelial P(i) transport is observed in both tissues. Also, in both epithelia, apically located sodium-dependent transport systems (Na+/P(i) and Na+/Si symport) represent major targets for known regulatory factors. By expression cloning using oocytes of Xenopus laevis, renal and small intestinal Na(+)-dependent phosphate and sulphate transport systems have been identified. Evidence has been obtained that cloned Na+/P(i) and Na+/Si symporters are localized in the apical membrane of proximal tubular or small intestinal epithelial cells respectively. Furthermore, recent results indicate that one of the cloned Na+/P(i) symporters is involved in the physiological and pathophysiological regulation of proximal tubular P(i) reabsorption.

Animals↗

PubMed1993

Expression cloning of rat renal Na+/SO4(2-) cotransport.

Injection of rat kidney cortex mRNA into Xenopus laevis oocytes leads to a stimulation of Na(+)-dependent SO4(2-) uptake. Based on this information, we have isolated from a corresponding library a cDNA (NaSi-1) that is most likely related to a Na+/SO4(2-) cotransport system. NaSi-1 cRNA leads in a time- and dose-dependent manner to specific stimulation of Na(+)-dependent SO4(2-) uptake in oocytes. The apparent affinity constants of the NaSi-1 cRNA-expressed transport resemble those of Na+/SO4(2-) cotransport in brush-border membrane. The NaSi-1 cDNA contains 2239 bp [including a poly(A) tail] and encodes a protein of 595 amino acids (66.05 kDa); the hydropathy profile suggests at least eight membrane-spanning regions. In vitro translation of NaSi-1 cRNA results in a protein of the expected size and suggests glycosylation. Northern blot analysis shows signals of 2.3 and 2.9 kb in kidney (more abundant in cortex than in papilla/medulla) and in mucosa of small intestine of rats. The above data indicate that we have structurally identified a membrane protein involved in renal and small-intestinal brush-border membrane Na+/SO4(2-) cotransport.

Amino Acid Sequence↗

PubMed1993

Expression of Na/Pi cotransport from opossum kidney cells in Xenopus laevis oocytes.

Xenopus laevis oocytes have been used for the expression of Na/Pi-cotransport activity by injections of poly(A)+ RNA (mRNA) isolated from an established renal cell line (OK cells). 3-5 days after mRNA injection, Na-dependent phosphate (Pi) uptake by oocytes was increased in a dose-dependent manner; there was no increase in Na-independent Pi uptake. Sucrose density-gradient fractionation indicated that the mRNA species encoding this activity is 2.4-2.8 kb in length. In Northern blots, using a cDNA probe related to human kidney-cortex Na/Pi-cotransport activity (NaPi-3), hybridization with a mRNA-species of 2.4-2.6 kb was obtained. Kinetic characterization ([Pi], [Na]) showed that expressed transport activity has properties similar to apical Na/Pi cotransport in OK cells.

Animals↗

PubMed1993

Expression cloning of a human renal cDNA that induces high affinity transport of L-cystine shared with dibasic amino acids in Xenopus oocytes.

A renal cDNA clone (rBAT) that induces system bo,+-like amino acid transport activity in Xenopus oocytes has recently been isolated (Bertran, J., Werner, A., Moore, M. L., Strange, G., Markovich, D., Biber, J., Testar, X., Zorzano, A., Palacín, and Murer, H. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 5601-5605). Here we show the isolation of a cDNA clone by screening a human kidney cortex cDNA library for expression of sodium-independent transport of L-[3H]arginine in Xenopus oocytes. The cRNA of this clone induces in oocytes, in addition to the uptake of L-arginine, that of L-[35S]cystine and L-[3H]leucine. Expressed uptake of these amino acids is mutually cis-inhibitable by the other 2 amino acids. Expressed uptake of L-cystine is saturable and shows an apparent Km in the micromolar range. All these characteristics resemble induction of system bo,+ related to rBAT in the oocytes. Human rBAT mRNA (approximately 2.5 kilobases) is found in kidney, small intestine (i.e., jejunum), pancreas, and liver. Human kidney poly(A)+ RNA (mRNA) induces sodium-independent uptake of L-cystine, L-arginine, and L-leucine in Xenopus oocytes. Hybrid depletion with an antisense oligonucleotide of the isolated clone greatly prevents (80-97%) human kidney mRNA-dependent induction of the uptake of these amino acids (i.e., L-cystine, L-arginine, and L-leucine). The isolated clone (2304 base pairs in length) contains a poly(A) tail and encodes a predicted 78.8-kDa protein which is 85 and 80% identical to the rabbit and rat rBAT, respectively. This predicted protein corresponds to a membrane glycoprotein, and contains six potential N-glycosylation sites which might be functional in the oocyte: [35S] methionine labeling of oocytes shows a specific band of 94 kDa in crude membranes of these human cRNA-injected oocytes; treatment of these oocytes with tunicamycin shifts the cRNA-specific translation product to approximately 72 kDa. We conclude that we have isolated a functional cDNA corresponding to human rBAT. The isolation of this human cDNA would lead to the study of the possible involvement of rBAT in human hyperaminoacidurias.

Amino Acid Sequence↗

PubMed1993

Expression cloning of human and rat renal cortex Na/Pi cotransport.

We have isolated two cDNA clones, NaPi-2 and NaPi-3, by screening rat kidney cortex and human kidney cortex cDNA libraries, respectively, for expression of sodium-dependent phosphate transport in Xenopus laevis oocytes. Substrate specificity and a detailed kinetic analysis (Na, Pi, H+ concentrations) suggested that expressed uptake activities relate to proximal tubular brush border membrane Na/Pi cotransport. NaPi-2 cDNA contains 2464 bp encoding a protein of 637 aa; NaPi-3 cDNA contains 2573 bp encoding a protein of 639 aa. NaPi-2- and NaPi-3-deduced protein sequences show high homology to each other but are different from the protein sequence deduced from the previously cloned NaPi-1 cDNA (from rabbit proximal tubules). Hydropathy profile predictions suggest at least eight membrane-spanning regions in NaPi-2/3-related proteins. In vitro translation results in proteins of the expected size and suggests glycosylation. Northern blot analysis shows corresponding mRNA species (approximately 2.7 kb) in kidney cortex of various species but no hybridization with RNAs isolated from a variety of other tissues (including intestinal segments); a hybridization signal (approximately 4.8 kb) was observed only in the lung (human). We conclude that we have structurally identified two closely related proteins most likely involved in human and rat renal brush border Na/Pi cotransport.

Amino Acid Sequence↗

PubMed1993

Two mRNA transcripts (rBAT-1 and rBAT-2) are involved in system b0,(+)-related amino acid transport.

Previously, we isolated a cDNA clone (rBAT-1) of 2.2 kilobase pairs (kb) from a rabbit kidney cortex cDNA library, encoding a protein involved in sodium-independent transport of L-dibasic amino acids, L-cystine, and some neutral amino acids via a system related to b0,(+)-like activity (Bertran, J., Werner, A., Moore, M. L., Stange, G., Markovich, D., Biber, J., Testar, X., Zorzano, A., Palacin, M., and Murer, H. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 5601-5605). In Northern blot hybridization using an rBAT-1 cDNA probe, 2.2- and 3.9-kb mRNA species were observed. Here we describe the isolation of a 3.9-kb cDNA clone (rBAT-2) by expression cloning using Xenopus laevis oocytes corresponding to the 3.9-kb mRNA species. On the basis of sequence analysis, in vitro translation (major protein of approximately 78 kDa), and functional analysis (expression of transport function), we conclude that rBAT-1- and rBAT-2-related proteins are identical: 677 amino acids in length, with most likely only one transmembrane-spanning domain. There are seven differences in the nucleotide composition within a common overlap of 2189 nucleotides, resulting in 2 amino acid replacements. In comparison with rBAT-1, rBAT-2 has 26 additional nucleotides at the 5'-end, an identical location of the first polyadenylation signal, and approximately 1.7 kb of 3'-untranslated sequence (rich in AT(U) motifs) prior to a poly(A) tail of 63 adenines. We conclude that rBAT-1 and rBAT-2 encode the same protein and that the major difference seems to be related to the use of different polyadenylation signals.

Amino Acid Sequence↗