Marketing de Relacionamento sob a influência da Internet

A evolução tecnológica favorece o surgimento de novas formas de oferta de produtos e serviços pelas empresas a seus clientes, acarretando efeitos sobre vários aspectos da organização e da sociedade. Um dos agentes que têm atuado nessa transformação é a Internet, por meio do comércio eletrônico. Como se posiciona o Marketing de Relacionamento quando as relações com o cliente passam a se dar prioritariamente pelo computador? Neste artigo, acentua-se a discussão sobre os elementos do Marketing de Relacionamento a serem gerenciados, contornados, assimilados ou aproveitados em benefício das empresas, trazidos pela Internet ou já presentes em sua realidade, porém sob influência do novo contexto, visando à manutenção ou desenvolvimento de vantagem competitiva nas empresas. Por meio de pesquisa exploratória na forma de estudo de multicasos com empresas atuantes no mercado consumidor, sediadas na Grande São Paulo, este estudo proporciona, enfim, uma reflexão acerca das práticas de Marketing de Relacionamento, da implementação de melhorias nos sites das empresas e das mútuas interferências entre as questões inerentes ao Marketing de Relacionamento e as operações pela internet.Technological advances favor new ways of offering products and services by companies to their clients thereby affecting various aspects of the organizations and society. One of the agents playing a role in this transformation is the Internet by means of electronic commerce. How does Relationship Marketing position itself when relations with the client become essentially carried out by means of the computer? A discussion is highlighted about the elements of Relationship Marketing to be managed, overcome, assimilated or used in benefit of the companies with results from the Internet or those already active, however under the influence of this new context, seeking to maintain or develop competitive advantages. An exploratory research was conducted in the form of a multicase study of consumer market companies in the São Paulo metropolitan area. A reflection is made about the practices of Relationship Marketing, the implementation on the company sites and on the mutual interferences between issues inherent to Relationship Marketing and Internet operations

A Non-Mammalian Type Opsin 5 Functions Dually in the Photoreceptive and Non-Photoreceptive Organs of Birds

A mammalian type opsin 5 (neuropsin) is a recently identified ultraviolet (UV)-sensitive pigment of the retina and other photosensitive organs in birds. Two other opsin 5-related molecules have been found in the genomes of non-mammalian vertebrates. However, their functions have not been examined as yet. Here, we identify the molecular properties of a second avian opsin 5, cOpn5L2 (chicken opsin 5-like 2), and its localization in the post-hatch chicken. Spectrophotometric analysis and radionucleotide-binding assay have revealed that cOpn5L2 is a UV-sensitive bistable pigment that couples with the Gi subtype of guanine nucleotide-binding protein (G protein). As a bistable pigment, it also shows the direct binding ability to agonist all-trans-retinal to activate G protein. The absorption maxima of UV-light-absorbing and visible light-absorbing forms were 350 and 521 nm, respectively. Expression analysis showed relatively high expression of cOpn5L2 mRNA in the adrenal gland, which is not photoreceptive but an endocrine organ, while lower expression was found in the brain and retina. At the protein level, cOpn5L2 immunoreactive cells were present in the chromaffin cells of the adrenal gland. In the brain, cOpn5L2 immunoreactive cells were found in the paraventricular and supraoptic nuclei of the anterior hypothalamus, known for photoreceptive deep brain areas. In the retina, cOpn5L2 protein was localized to subsets of cells in the ganglion cell layer and the inner nuclear layer. These results suggest that the non-mammalian type opsin 5 (Opn5L2) functions as a second UV sensor in the photoreceptive organs, while it might function as chemosensor using its direct binding ability to agonist all-trans-retinal in non-photoreceptive organs such as the adrenal gland of birds

Lealdade em Compras Online versus Offline: reflexões sobre os fatores relevantes

O objetivo deste estudo foi identifi car aspectos relevantes para a lealdade dos clientes ao fornecedor e ao canal de comercialização, especifi camente nas possíveis diferenças entre os que compram e os que não compram por meio da Internet. Para tanto, além da revisão da literatura pertinente, foi realizada uma pesquisa qualitativa com 30 compradores de livros, CDs e DVDs. Os resultados indicam que os maiores atrativos do canal online são a praticidade e a comodidade e, como fatores desestimulantes, a confi abilidade e os aspectos fi nanceiros relativos. Em relação à lealdade ao fornecedor, no canal físico, foram citados o atendimento dos vendedores, a localização da loja/facilidade de acesso, a satisfação com experiência anterior de compra e a competitividade de preços. No canal online, os aspectos mais importantes foram a satisfação com a experiência anterior de compra, a disponibilidade das informações sobre produtos e a competitividade de preços

Evolution of mammalian Opn5 as a specialized UV-absorbing pigment by a single amino acid mutation.

Opn5 is one of the recently identified opsin groups that is responsible for nonvisual photoreception in animals. We previously showed that a chicken homolog of mammalian Opn5 (Opn5m) is a Gi-coupled UV sensor having molecular properties typical of bistable pigments. Here we demonstrated that mammalian Opn5m evolved to be a more specialized photosensor by losing one of the characteristics of bistable pigments, direct binding of all-trans-retinal. We first confirmed that Opn5m proteins in zebrafish, Xenopus tropicalis, mouse, and human are also UV-sensitive pigments. Then we found that only mammalian Opn5m proteins lack the ability to directly bind all-trans-retinal. Mutational analysis showed that these characteristics were acquired by a single amino acid replacement at position 168. By comparing the expression patterns of Opn5m between mammals and chicken, we found that, like chicken Opn5m, mammalian Opn5m was localized in the ganglion cell layer and inner nuclear layer of the retina. However, the mouse and primate (common marmoset) opsins were distributed not in the posterior hypothalamus (including the region along the third ventricle) where chicken Opn5m is localized, but in the preoptic hypothalamus. Interestingly, RPE65, an essential enzyme for forming 11-cis-retinal in the visual cycle is expressed near the preoptic hypothalamus of the mouse and common marmoset brain but not near the region of the chicken brain where chicken Opn5m is expressed. Therefore, mammalian Opn5m may work exclusively as a short wavelength sensor in the brain as well as in the retina with the assistance of an 11-cis-retinal-supplying system

Opsin 3-Related Genes in Chicken Retina and Brain

Opsin family genes encode G protein-coupled seven-transmembrane proteins that bind a retinaldehyde chromophore in photoreception. Here, we sought potential as yet undescribed avian retinal photoreceptors, focusing on Opsin 3 homologs in the chicken. We found two Opsin 3-related genes in the chicken genome: one corresponding to encephalopsin/panopsin (Opn3) in mammals, and the other belonging to the teleost multiple tissue opsin (TMT) 2 group. Bioluminescence imaging and G protein activation assays demonstrated that the chicken TMT opsin (cTMT) functions as a blue light sensor when forced-expressed in mammalian cultured cells. We did not detect evidence of light sensitivity for the chicken Opn3 (cOpn3). In situ hybridization demonstrated expression of cTMT in subsets of differentiating cells in the inner retina and, as development progressed, predominant localization to retinal horizontal cells (HCs). Immunohistochemistry (IHC) revealed cTMT in HCs as well as in small numbers of cells in the ganglion and inner nuclear layers of the post-hatch chicken retina. In contrast, cOpn3-IR cells were found in distinct subsets of cells in the inner nuclear layer. cTMT-IR cells were also found in subsets of cells in the hypothalamus. Finally, we found differential distribution of cOpn3 and cTMT proteins in specific cells of the cerebellum. The present results suggest that a novel TMT-type opsin 3 may function as a photoreceptor in the chicken retina and brain

Opn5L1 is a retinal receptor that behaves as a reverse and self-regenerating photoreceptor

Most opsins are G protein-coupled receptors that utilize retinal both as a ligand and as a chromophore. Opsins’ main established mechanism is light-triggered activation through retinal 11-cis-to-all-trans photoisomerization. Here we report a vertebrate non-visual opsin that functions as a Gi-coupled retinal receptor that is deactivated by light and can thermally self-regenerate. This opsin, Opn5L1, binds exclusively to all-trans-retinal. More interestingly, the light-induced deactivation through retinal trans-to-cis isomerization is followed by formation of a covalent adduct between retinal and a nearby cysteine, which breaks the retinal-conjugated double bond system, probably at the C11 position, resulting in thermal re-isomerization to all-trans-retinal. Thus, Opn5L1 acts as a reverse photoreceptor. We conclude that, like vertebrate rhodopsin, Opn5L1 is a unidirectional optical switch optimized from an ancestral bidirectional optical switch, such as invertebrate rhodopsin, to increase the S/N ratio of the signal transduction, although the direction of optimization is opposite to that of vertebrate rhodopsin