SEARCH · PubMed Health

Results for “Transient expression”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 379 records · Page 21Linked to original sources

PubMed1987

Transient expression of 5-HT1A receptor binding sites in some areas of the rat CNS during postnatal development.

The developmental evolution of 5-HT1A receptor binding sites was examined in the rat CNS during the early postnatal period using quantitative autoradiography and binding assays with 3H-8-OH-DPAT as the selective ligand. A progressive increase in the density of 5-HT1A sites was observed in the hippocampus, septum and cerebral cortex, up to adult levels which were reached around the third postnatal week. In contrast, complex biphasic (increase then decrease) changes were noted in other structures (for instance the nucleus of the lateral lemniscus), and even a progressive decrease in the density of 5-HT1A sites took place in the cerebellum during the first two postnatal weeks. The transient expression of 5-HT1A receptor binding sites in a structure such as the cerebellum which develops exclusively for the postnatal period further supports that 5-HT might play a trophic role during maturation of the CNS.

8-Hydroxy-2-(di-n-propylamino)tetralin↗

PubMed1995

Transient expression of calcium-independent nitric oxide synthase in blood vessels during brain development.

The calcium-independent nitric oxide synthase, known as NOS-II or inducible NOS, is only present in adult brain during pathologies that involve inflammatory events. We sought to establish whether NOS-II was also expressed in the course of normal brain development. NOS-II mRNA, measured by quantitative polymerase chain reaction, appeared during the perinatal period in different brain areas. It was detected on embryonic day 14, the earliest time analyzed, and then levels decayed until the first postnatal week when a second, more robust phase of expression arose to peak around postnatal day 7. Expression then declined to negligible levels in adulthood. Immunohistology revealed translation of the NOS-II protein in both embryonic and postnatal animals, localized to parenchymal blood vessels, whereas no vessel staining was detected in adults. Furthermore, NOS-II mRNA and enzymatic activities were present in isolated brain microvessels from developing animals but not from adults, and P7 vessels contained a 125 kDa protein band detected with a monoclonal antibody raised against rat NOS-II protein. These results indicate that the calcium-independent NOS mRNA and functional protein are transiently expressed in vessels throughout the brain in the course of normal development.

Animals↗

PubMedDate not supplied

Transient expression of RSVCAT in transgenic zebrafish made by electroporation.

We report the fish use of an exponential decay electroporation system to introduce foreign DNA into fertilized zebrafish embryos. The plasmid RSVCAT (Rous sarcoma viral promoter (RSV) upstream from the chloramphenicol acetyltransferase gene (CAT)) was linearized and introduced into fertile zebrafish embryos by electroporation no later than the four-cell stage. Conditions for the procedure were empirically derived, and 68% of the treated animals survived through hatching to at least 6 days after fertilization and well beyond. Dot-blot analysis on DNA extracted from individual hatching fry demonstrated that 65% of the animals tested carried the foreign construct. Enzyme assays on the soluble proteins of treated animals were positive for chloramphenicol acetyltransferase activity. These data demonstrate that the foreign construct was being transiently expressed in the developing tissues of the embryo. The simplicity of this technique will greatly enhance the ability to analyze gene promoter regulation in vivo in transgenic zebrafish. The ability of the electroporated DNA to integrate into the host genome and to generate stable lines of transgenic fish is discussed.

Animals↗

PubMed2005

Temporal and transient expression of olive enoyl-ACP reductase gene during flower and fruit development.

Enoyl-ACP reductase is a catalytic component of the fatty acid synthetase (FAS) type II system in plants that is involved in the de novo fatty acid biosynthesis in plastids. A cDNA encoding an enoyl-ACP reductase responsible for the removal of the trans-unsaturated double bonds to form saturated acyl-ACP has been isolated from a library made from ripening fruits of Olea europaea L. The predicted protein contains 393 amino acid residues including a consensus chloroplast specific transit peptide. A strong homology was observed when olive enoyl-ACP reductase aligned with other plant sequences. Southern hybridization analysis revealed that enoyl-ACP reductase is encoded by a single gene in olives. Northern hybridization showed a transient expression of the enoyl-ACP reductase (ENR) gene at early stages of drupe (5-7 weeks after flowering, WAF), embryo and endosperm (13-16 WAF) while in mesocarp (13-19 WAF) the expression remained at high levels. In situ hybridization showed particularly prominent expression in the palisade and vascular tissue of young leaves, the tapetum, developing pollen grains and vascular tissue of anthers and to less extent in the embryo sac and transmitting tissue of the carpel. The distinctive spatial and temporal regulation of the ENR gene is consistent with major roles, not only in thylakoid membrane formation and fatty acid deposition, but also in the provision of precursor molecules for the biosynthesis of oxilipins that are important in plant tissues involved in transportation and reproduction.

Amino Acid Sequence↗

PubMed1991

The Drosophila homologue of vertebrate myogenic-determination genes encodes a transiently expressed nuclear protein marking primary myogenic cells.

We have isolated a cDNA clone, called Dmyd for Drosophila myogenic-determination gene, that encodes a protein with structural and functional characteristics similar to the members of the vertebrate MyoD family. Dmyd clone encodes a polypeptide of 332 amino acids with 82% identity to MyoD in the 41 amino acids of the putative helix-loop-helix region and 100% identity in the 13 amino acids of the basic domain proposed to contain the essential recognition code for muscle-specific gene activation. Low-stringency hybridizations indicate that Dmyd is not a member of a multigene family similar to MyoD in vertebrates. Dmyd is a nuclear protein in Drosophila, consistent with its role as a nuclear-gene regulatory factor, and is proposed to be a transiently expressed marker for muscle founder cells. We have used an 8-kilobase promoter fragment from the gene, which contains the first 55 amino acids of the Dmyd protein, joined to lacZ, to follow myogenic precursor cells into muscle fibers with antibodies to beta-galactosidase and to Dmyd. Unlike the myogenic factors in vertebrate muscle cells, Dmyd appears to be expressed at a much lower level in differentiated Drosophila muscles, so Dmyd cannot be followed continuously as a muscle marker. This fact is reflected in the loss of Dmyd RNA expression in 12- to 24-hr embryos, a major period of early myogenesis, as well as in the undetectable level of the nuclear antigen in primary cultures of embryonic and adult Drosophila muscle.

Age Factors↗

PubMed1991

Development of cholinesterase histochemical staining in cerebellar cortex: transient expression of "nonspecific" cholinesterase in Purkinje cells of the nodulus and uvula.

Patterns of "nonspecific" cholinesterase (ChE) and acetylcholinesterase (AChE) activity were studied in developing rat cerebellar cortex by enzyme histochemistry and light and electron microscopy. Three types of ChE histochemical reaction product were observed in cerebellar cortex: (i) ChE is found in capillary endothelium throughout the cerebellum. Capillary ChE staining is present by the time of birth and continues into adulthood. (ii) ChE is found in radial glial fibers and their parent cell bodies, the Golgi epithelial cells. Radial glial fiber staining is mot intense during the first 3 weeks of postnatal life. (iii) ChE is found in Purkinje cells of the nodulus and ventral uvula. No ChE staining of Purkinje cells was seen in other parts of the cerebellum. ChE staining of Purkinje cells appears to be transient, first appearing at Postnatal Day 2 (P2), reaching peak intensity at P7-9, and decreasing to adult levels by P16. AChE activity displays a pattern markedly different from ChE, with staining in deep cerebellar nuclei, in putative mossy fiber terminals, and in Golgi neurons of cerebellar cortex. No evidence was found for transient AChE staining in Purkinje cells in any part of the cerebellum. The function of transiently expressed ChE activity in developing Purkinje neurons is unknown, but may be related to reorganization of cerebellar cortical circuitry associated with growth of mossy fiber afferents.

Acetylcholinesterase↗

PubMed1987

Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds.

A cDNA clone for a cysteine proteinase inhibitor of rice (oryzacystatin) was isolated from a lambda gt10 cDNA library of rice immature seeds by screening with synthesized oligonucleotide probes based on partial amino acid sequences of oryzacystatin. A nearly full-length cDNA clone was obtained which encoded 102-amino acid residues. The amino acid sequence of oryzacystatin deduced from the cDNA sequence was significantly homologous to those of mammalian cystatins, especially family 2 cystatins. Oryzacystatin contained the sequence Gln-Val-Val-Ala-Gly conserved among most members of the cystatin superfamily. The gene for oryzacystatin was transcribed into a single mRNA species of about 700 nucleotides. The content of mRNA reached its highest level 2 weeks after flowering and then gradually decreased to undetectable levels at 10 weeks. This feature of transient expression is coordinate with that of glutelin (a major storage protein), although the expression of oryzacystatin precedes that of glutelin by about 1 week.

Amino Acid Sequence↗

PubMed2005

Transient expression of laminin alpha1 chain in regenerating murine liver: restricted localization of laminin chains and nidogen-1.

Most interstitia between epithelial and endothelial cells contain basal laminae (BLs), as defined by electron microscopy. However, in liver, the sinusoidal interstitium (called space of Disse) between hepatocytes and sinusoidal endothelial cells (SECs) lacks BLs. Because laminins are major components of BLs throughout the body, whether laminins exist in sinusoids has been a controversial issue. Despite recent advances, the distribution and expression of laminin chains have not been well defined in mammalian liver. Here, using a panel of antibodies, we examined laminins in normal and regenerating mouse livers. Of alpha chains, alpha5 was widely observed in all BLs except for sinusoids, while the other alpha chains were variously expressed in Glisson's sheath and central veins. Laminin gamma1 was also distributed to all BLs except for sinusoids. Although the beta2 chain was observed in all BLs and sinusoids, the expression of beta1 chain was restricted to Glisson's sheath. Detailed analysis of regenerating liver revealed that alpha1 and gamma1 chains appeared in sinusoids and were produced by stellate cells. The staining of alpha1 and gamma1 chains reached its maximum intensity at 6 days after two-thirds partial hepatectomy (PHx). Moreover, in vitro studies showed that alpha1-containing laminin promoted spreading of sinusoidal endothelial cells (SECs) isolated from normal liver, but not other hepatic cells. In addition, SECs isolated from regenerating liver elongated pseudopodia on alpha1-containing laminin more so than did cells from normal liver. The transient expression of laminin alpha1 may promote formation of sinusoids after PHx.

Animals↗

PubMed1990

Transient expression of neurofilament protein during hair cell development in the mouse cochlea.

A polyclonal antiserum raised against the 145 kDa neurofilament protein (NFM) has been used to study the distribution of neurofilaments both in organotypic cultures of the early postnatal mouse cochlea and during development of the mouse cochlea in vivo. In the cultures, both the inner hair cells and the outer hair cells are stained by the antibodies, as well as the innervating afferent fibres from the spiral ganglion. In cultures denervated at the time of preparation, neurofilament positive hair cells can still be detected after 7 days in vitro. NFM can also be detected by immunoblotting in such denervated cultures. Characteristic 10 nm diameter, cytoplasmic filaments can also be observed in cultured hair cells using transmission electron microscopy. Immunostaining of cryosections prepared from cochleas at embryonic days 17 and 19, and days 1, 2, 5, 10 and 21 post-partum reveals that hair cells transiently express NFM during their development in vivo. Expression of NFM in hair cells is first detected at embryonic day 19 in the basal region of the cochlea and, by 2 days post-partum, neurofilament positive hair cells are found throughout the entire length of the cochlea. By 10 days post-partum, staining of hair cells begins to diminish and, by 21 days post-partum, NFM can no longer be detected in hair cells.

Animals↗

PubMed1997

Olfaction: transient expression of a putative odorant receptor in the avian notochord.

In vertebrates, odors are thought to be detected by a multigene family encoding several hundreds of seven-transmembrane-domain G-protein-coupled receptors found in fish, rat, mouse, dog, and human. Recently, the putative odorant receptor (OR) gene family in the chicken has been characterized. Twelve members have been isolated and subdivided into six subfamilies. Herein, we have further characterized the chicken olfactory receptor subfamily 7 (COR7) composed of two highly related genes (named COR7a and COR7b) which are 98.5% identical. By in situ hybridization experiments, both COR7a and COR7b transcripts were detected in the olfactory epithelium from embryonic day 6 (E6) to the new born stage. Within the olfactory epithelium, the spatial distribution of COR7a and COR7b labeled cells was random. We also observed that every individual positive cell did not coexpress the COR7a and COR7b genes. Interestingly, the COR7b gene was found to be transiently expressed in the notochord from E2 to E6, whereas COR7a or any of the other known members of the COR gene family were not detected in this mesodermal tissue. These data suggest that, in addition to its potential role as an OR in the olfactory system, COR7b may also have a function in the notochord that is essential for the dorsoventral organization of the neural tube and of the somitic mesoderm. We also discuss the possible role(s) of a putative OR present in both the notochord and the sensory olfactory epithelium.

Amino Acid Sequence↗

PubMed1991

Early appearance and transient expression of vasopressin receptors in the brain of rat fetus and infant. An autoradiographical and electrophysiological study.

The development of vasopressin (AVP) receptors in the rat brain, spinal cord and pituitary gland was studied by in vitro light microscopic autoradiography. AVP binding sites were labeled using [3H]AVP in tissue sections from animals aged between embryonic day 12 (E12) and postnatal day 90 (PN90); the binding of [3H]AVP to oxytocin receptors was prevented by adding in the incubation medium a highly selective oxytocin agonist. Specific binding was first detected at E16 in the ventral pontine reticular formation. Many other brain areas were progressively labeled between E18 and PN5. The distribution of binding sites observed at PN5 remained unchanged until the beginning of the third postnatal week. Thereafter binding was markedly reduced or even disappeared in several areas, in particular in the facial nucleus. The adult distribution of AVP binding sites was established at the time of weaning. The properties of transient AVP binding sites in the facial nucleus were studied both by autoradiography and by electrophysiology. Non-radioactive AVP displaced [3H]AVP binding in this nucleus as efficiently as it did in the lateral septum of the adult. Single-unit extracellular recordings showed that AVP can excite facial motoneurones by interacting with receptors which are pharmacologically indistinguishable from V1 (vasopressor) type. Thus, AVP binding sites transiently expressed in the brain of fetal and infant rat probably represent functional neuronal receptors, having the same ligand selectivity and affinity than AVP binding sites present in the adult. This suggests that AVP acts not only as a neuropeptide in the adult brain but may play a significant role during maturation of the central nervous system.

Action Potentials↗

PubMed1992

PsiB, and anti-SOS protein, is transiently expressed by the F sex factor during its transmission to an Escherichia coli K-12 recipient.

PsiB, an anti-SOS protein, shown previously to prevent activation of RecA protein, was purified from the crude extract of PsiB overproducing cells. PsiB is probably a tetrameric protein, whose subunit has a sequence-deduced molecular mass of 15741 daltons. Using an immuno-assay with anti-PsiB antibodies, we have monitored PsiB cell concentrations produced by F and R6-5 plasmids: the latter type produces a detectable level of PsiB protein while the former does not. The discrepancy can be assigned to a Tn10 out-going promoter located upstream of psiB. When we inserted a Tn10 promoter upstream of F psiB, the F PsiB protein concentration reached the level of R6-5 PsiB. We describe here the physiological role that PsiB protein may have in the cell and how it causes an anti-SOS function. We observed that PsiB protein was transiently expressed by a wild-type F sex factor during its transmission to an Escherichia coli K-12 recipient. In an F+ x F- cross, PsiB concentration increased at least 10-fold in F- recipient bacteria after 90 minutes and declined thereafter; the psiB gene may be repressed when F plasmid replicates vegetatively. PsiB protein may be induced zygotically so as to protect F single-stranded DNA transferred upon conjugation. PsiB protein, when overproduced, may interfere with RecA protein at chromosomal single-stranded DNA sites generated by discontinuous DNA replication, thus causing an SOS inhibitory phenotype.

Bacterial Proteins↗

PubMed1996

Transient expression of stromelysin-3 mRNA in the amphibian small intestine during metamorphosis.

It has been suggested that a matrix metalloproteinase, stromelysin-3 (ST3), is an important enzyme for epithelial transformation; the ST3 gene is known to be regulated by thyroid hormone during Xenopus metamorphosis. In this study, we have examined the distribution of ST3 mRNA in the small intestine of Xenopus during metamorphosis by using in situ hybridization. Around stage 58, ST3 mRNA is first detectable in larval fibroblasts near the muscular layer, and then increases in amount throughout the entire region of connective tissue. By stage 61, when connective tissue cells are rapidly increasing in number, ST3 mRNA is localized in fibroblasts just beneath the epithelium. This localization of ST3 mRNA is in good temporal accordance with modification of the basement membrane and epithelial transformation from the larval to adult form. Thereafter, ST3 mRNA gradually decreases and is no longer detected after stage 63 when the adult epithelium has completely replaced the larval type. The transient expression of ST3 mRNA in the fibroblasts of connective tissue during metamorphosis indicates that it plays an important role in epithelial transformation by changing the basement membrane.

Animals↗

PubMed1997

Transient expression of the Drosophila melanogaster cinnabar gene rescues eye color in the white eye (WE) strain of Aedes aegypti.

The lack of eye pigment in the Aedes aegypti WE (white eye) colony was confirmed to be due to a mutation in the kynurenine hydroxylase gene, which catalyzes one of the steps in the metabolic synthesis of ommochrome eye pigments. Partial restoration of eye color (orange to red phenotype) in pupae and adults occurred in both sexes when first or second instar larvae were reared in water containing 3-hydroxykynurenine, the metabolic product of the enzyme kynurenine hydroxylase. No eye color restoration was observed when larvae were reared in water containing kynurenine sulfate, the precursor of 3-hydroxykynurenine in the ommochrome synthesis pathway. In addition, a plasmid clone containing the wild type Drosophila melanogaster gene encoding kynurenine hydroxylase, cinnabar (cn), was also able to complement the kynurenine hydroxylase mutation when it was injected into embryos of the A. aegypti WE strain. The ability to complement this A. aegypti mutant with the transiently expressed D. melanogaster cinnabar gene supports the value of this gene as a transformation reporter for use with A. aegypti WE and possibly other Diptera with null mutations in the kynurenine hydroxylase gene.

Aedes↗

PubMed1997

A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development.

To study the role of matrix metalloproteinases (MMPs) in early vertebrate development, we cloned cDNAs for six different MMPs from the frog Xenopus laevis embryos at different stages of development and describe here a novel MMP called XMMP. Xenopus XMMP has 604 amino acids including a putative signal peptide of 22 residues. At the carboxyl-terminal end of the propeptide, XMMP has a 37-amino acid-long insertion domain containing a segment that is 38% identical with a rat vitronectin sequence between residues 108-135. Following this domain is an RRKR motif, a putative cleavage site for intracellular activation by furin proteinases. XMMP lacks a proline-rich linker peptide, or hinge region, typically found in other MMPs between the catalytic domain and carboxyl-terminal "hemopexin/vitronectin-like" domain. In XMMP, the carboxyl-terminal domain is composed of four tandem repeats that are 21-33% identical to a sequence (residues 213-264) encoded by vitronectin exon-5. Interestingly, XMMP gene is transiently expressed during Xenopus embryo development. XMMP mRNA of 3.0 kilobase pairs was undetected in the blastula stage embryo, induced in gastrula embryo, expressed in neurula embryo, and then down-regulated in pretailbud embryo. In comparison, other Xenopus MMP genes that we have cloned show a different developmental regulation. In blastula embryo, the only MMP gene expressed was found to be 92-kDa type IV collagenase, which was also expressed in the gastrula, neurula, and pretailbud embryos. Expression of stromelysin-1, stromelysin-3, and two different membrane type-MMPs was first detected in the neurula and pretailbud embryos. These results suggest that MMPs and the novel XMMP reported here play a role in Xenopus early development.

Amino Acid Sequence↗

PubMed1995

The cDNA cloning and transient expression of a chicken gene encoding a 3 beta-hydroxysteroid dehydrogenase/delta 5-->4 isomerase unique to major steroidogenic tissues.

Two cDNA clones, on containing a 2.7-kb and the other a 1.6-kb insert, were obtained from a chicken adrenal gland cDNA library by screening with a partial chicken cDNA fragment generated by PCR. Primers were used that corresponded to conserved regions among several published cDNA sequences of mammalian 3 beta-hydroxysteroid dehydrogenase/delta 5-->4 isomerase (3 beta-HSD). Both clones contained the same open reading frame (ORF) encoding 377 amino acids (aa). The difference in their sizes was due to the use of different polyadenylation sites. The deduced aa sequence showed 54-57% overall identity with those of the human, macaque, bovine, mouse, rat and rainbow trout 3 beta-HSD. A 9-aa stretch (FYYISDDTP) is conserved among the chicken, mammalian and rainbow trout 3 beta-HSD, suggesting that it is essential for enzymatic activity. Northern blot hybridization demonstrated the presence of two types of mRNA, corresponding to the above two cDNA classes, in the adrenal gland, ovary and testis. Transient expression of the chicken ORF in COS-7 cells demonstrated coupled dehydrogenase and isomerase activities of 3 beta-HSD on three different substrates; pregnenolone, 17 alpha-hydroxypregnenolone and dehydroepiandrosterone. Among the Km values determined for the three substrates, that for dehydroepiandrosterone was the lowest, which was different from the case for human 3 beta-HSD.

3-Hydroxysteroid Dehydrogenases↗

PubMed1992

N-methyl-D-aspartate receptors are transiently expressed in the developing spinal cord ventral horn.

Quantitative receptor autoradiography was used to map the distribution of N-methyl-D-aspartate (NMDA) receptors in the developing rat spinal cord. Three different specific ligands, which label partially overlapping subpopulations of NMDA receptors, were used: an agonist (L-[3H]glutamate), a noncompetitive antagonist ([3H]MK-801), and a competitive antagonist ([3H]CGP-39653). In the adult, NMDA receptors labeled with all three ligands are restricted to the substantia gelatinosa in the spinal dorsal horn. In marked distinction, at postnatal day 7 NMDA receptors labeled with L-[3H]glutamate and [3H]MK-801 are present throughout the spinal gray matter. NMDA receptors in the neonatal spinal ventral horn have a higher affinity for L-[3H]glutamate than those in the adult substantia gelatinosa. Over the second and third postnatal weeks, NMDA receptors are lost from all areas of the spinal gray matter except for the substantia gelatinosa. Neonatal NMDA receptors identified with [3H]CGP-39653 are restricted to the substantia gelatinosa. These results show that the immature ventral horn contains a subpopulation of NMDA receptors and raise the possibility that motor neurons transiently express NMDA receptors in early postnatal life. Ventral horn NMDA receptors may be a component of the mechanisms by which the mature phenotype of motor neurons is acquired through activity-dependent processes. The loss of NMDA receptors over the course of development may play a role in limiting the period of motor neuron plasticity.

2-Amino-5-phosphonovalerate↗

PubMed1989

Transient expression of human immunodeficiency virus type 1 genome results in a nonproductive infection in human fetal dorsal root ganglia glial cells.

Human immunodeficiency virus type 1 (HIV-1), the etiologic agent of acquired immunodeficiency syndrome (AIDS), has been implicated in the generation of AIDS-associated neurologic dysfunction. We are currently examining the replicative processes involved in HIV-1 infection of selected human fetal neural cell populations in vitro. To determine whether infection of the human fetal dorsal root ganglia (DRG) glial cell population culminates in the production and release of infectious HIV-1, cocultivation and reverse transcriptase (RT) assays were performed. Direct assay of HIV-1 infected neural cell supernatants as well as exposure of permissive SupT1 cells to these HIV-1-infected neural cell supernatants detected no RT activity in either the HIV-1-infected DRG glial cell supernatants or the SupT1 cell supernatants. When SupT1 cells were cocultivated with the HIV-1-infected neural cells for 24-hr intervals, RT activity was detected in the SupT1 supernatants from cocultures initiated less than 2 days after infection (most likely resulting from infectious input virus) but not from cocultures initiated on 3, 5, 10, and 30 days after infection. Hybridization analysis demonstrated transient expression of HIV-1 cytoplasmic mRNA with accumulation reaching a maximum level by 2 to 3 days postinfection, declining thereafter with low, but detectable, levels at 16 days postinfection. In addition, polymerase chain reaction amplification in conjunction with DNA blot hybridization detected HIV-1-specific proviral DNA at 3 days postinfection. Cumulatively, these data suggest that HIV-1 infection of human fetal DRG glial cells culminates in a nonproductive infection with expression of at least a fraction of the virus genome but no detectable infectious virus production.

Cells, Cultured↗