Leaflet anatomy of Poiretia Vent. (Leguminosae, Papilionoideae, Dalbergieae) with emphasis on internal secretory structures in support of taxonomy

Flora ◽  
2019 ◽  
Vol 260 ◽  
pp. 151484 ◽  
Author(s):  
Katiane Reis Mendes ◽  
Ana Paula Fortuna-Perez ◽  
Tatiane Maria Rodrigues
1986 ◽  
Vol 97 (7-8) ◽  
pp. 479-487
Author(s):  
Chaitali Chakrabarty ◽  
P. K. Mukherjee
Keyword(s):  

2021 ◽  
Vol 95 ◽  
pp. 104224
Author(s):  
Suzana Marques Barbosa ◽  
Natalia do Couto Abreu ◽  
Mozaniel Santana de Oliveira ◽  
Jorddy Nevez Cruz ◽  
Eloisa Helena de Aguiar Andrade ◽  
...  

2005 ◽  
Vol 83 (3) ◽  
pp. 279-286 ◽  
Author(s):  
Carlos André Espolador Leitão ◽  
Renata Maria Strozi Alves Meira ◽  
Aristéa Alves Azevedo ◽  
João Marcos de Araújo ◽  
Kellen Lagares Ferreira Silva ◽  
...  

Triumfetta semitriloba Jacq. (Tiliaceae) is a tropical weedy species with floral nectaries and glands located at the margins of the leaves. The objectives of this work were to describe the anatomy of these secretory structures and to analyze their exudates. Sucrose, glucose, and fructose were identified in the product released by these secretory structures, characterizing them as nectaries. The nectaries of T. semitriloba are of a specialized type; a secretory epidermis comprised of pluricellular and multiserial nectariferous trichomes covers a nectariferous parenchyma, vascularized by phloem and xylem. A mass of phenolic compounds occurs in the head cells of the nectariferous trichomes of the foliar and bract nectaries; however, it is absent in trichomes of the floral nectary. The leaf and bract nectaries differed from those from flowers in their length and diameter. Structural features of the nectaries of T. semitriloba are typical of other taxa of the Malvales.Key words: foliar anatomy, histochemistry, Malvales, nectaries, Tiliaceae, Triumfetta semitriloba.


1991 ◽  
Vol 111 (3) ◽  
pp. 407-410
Author(s):  
B. N. Tsibel' ◽  
A. Ya. Terner ◽  
L. Yu. Raevskaya ◽  
L. S. Vasil'eva

2016 ◽  
Vol 203 (1) ◽  
pp. 29-54 ◽  
Author(s):  
Hanan H. Abd-Elhafeez ◽  
Doaa M. Mokhtar ◽  
Ahmed H.S. Hassan

Telocytes (TCs) are a special type of interstitial cell with characteristic cellular processes that are described in many organs. The current study aimed to investigate TCs in seminal vesicles of the Soay ram responding to melatonin treatment during the nonbreeding season by conventional immunohistochemical stains, and to detect the ultrastructural and morphometrical changes of TCs. TCs in the control group showed a broad range of staining affinity and also reacted positively to CD117/c-kit, CD34, desmin, S-100 protein, and progesterone and estrogen receptors alpha, while after melatonin treatment a strong reaction against these 6 antibodies was recorded. Electron microscopically, TCs in the control group were characterized by a small cell body with distinct long cytoplasmic extensions called telopodes (Tps). Tps had alternation of the thin segment (podomers) and dilated segments (podoms), in which the latter accommodate mitochondria, rough endoplasmic reticulum and caveolae. TCs and their Tps were interconnected by homo- and heterocellular junctions and form a wide network to communicate between different cell types. Tps showed close contact with immune cells, progenitor stem cells, smooth muscle cells and other interstitial cells. Melatonin caused a significant increase in the number of TCs, length of Tps, and number and diameter of secretory vesicles. Also, the melatonin-treated group showed exaggerated secretory activity in the form of a massive release of secretory vesicles from Tps. Moreover, Tps showed an increase in their contact with blood and lymphatic capillaries, nerve endings and Schwann cells. In addition, the shedding of secretory structures (exosomes, ectosomes, and multivesicular bodies) was greater from Tps, which were involved in paracrine signaling in the melatonin-treated group. The length and ramifications of Tps together with the intercellular junctions and the releasing of shed vesicles or exosomes assumed an essential role of TCs in intercellular signaling and coordination. On the basis of their distribution and morphology, we investigated whether the different locations of TCs could be associated with different roles.


Flora ◽  
2016 ◽  
Vol 220 ◽  
pp. 52-62 ◽  
Author(s):  
Karina Bertechine Gagliardi ◽  
Inês Cordeiro ◽  
Diego Demarco
Keyword(s):  

2014 ◽  
Vol 8 (27) ◽  
pp. 947-952 ◽  
Author(s):  
Filho, S.C. Vasconcelos ◽  
A.L.L. Ferreira, ◽  
J.M. Vasconcelos, ◽  
L.S. SILVA, ◽  
L.C.S. Pereira,
Keyword(s):  

2004 ◽  
Vol 52 (1) ◽  
pp. 51-57 ◽  
Author(s):  
STEFANIA BOTTEGA ◽  
FABIO GARBARI ◽  
ANNA MARIA PAGNI
Keyword(s):  

1993 ◽  
Vol 41 (2) ◽  
pp. 193-203 ◽  
Author(s):  
P Bianco ◽  
M Riminucci ◽  
G Silvestrini ◽  
E Bonucci ◽  
J D Termine ◽  
...  

Bone sialoprotein (BSP), a bone matrix-enriched glycoprotein containing the Arg-Gly-Asp (RGD) motif and endowed with cell binding properties, was localized in osteoblasts and early bone matrix of developing rat bone at the ultrastructural level. Preliminary light microscopic observations indicated that intracellular labelling was restricted to a paranuclear dot corresponding to the "negative Golgi image" of classical histology. The same pattern was observed whether antisera against the fully glycosylated protein or a peptide antiserum to a stretch of amino acids in human BSP sequence were employed. At the EM level, we obtained labeling over the Golgi area of osteoblasts but not over the rER. The labeling was concentrated over distensions of the trans Golgi and over pro-secretory granules. In the matrix, BSP was distributed in a non-random manner. The label was concentrated over spherical aggregates of finely fibrillar material corresponding to the sites of early mineral deposition (so-called "mineralization nodules"). Such BSP-positive foci were seen both close to and away from the cell surface. The predominant association of BSP with Golgi and post-Golgi secretory structures and its absence from rER, as well as the reproducibility of the same pattern of localization with different antisera, might indicate a slow transit of the protein through the Golgi, not necessarily associated with protein glycosylation.


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