Production planning of a flexible manufacturing system in a material requirements planning environment

Early flexible manufacturing system (FMS) production planning models exhibited a variety of planning objectives; typically, these objectives were independent of the overall production environment. More recently, some researchers have proposed hierarchical production planning and scheduling models for FMS. In this article, we examine production planning of FMS in a material requirements planning (MRP) environment. We propose a hierarchical structure that integrates FMS production planning into a closed-loop MRP system. This structure gives rise to the FMS/MRP rough-cut capacity planning (FMRCP) problem, the FMS/MRP grouping and loading (FMGL) problem, and the FMS/MRP detailed scheduling problem. We examine the FMRCP and FMGL problems in detail and present mathematical programming models for each of these problems. In particular, the FMRCP problem is modeled as a generalized assignment problem (GAP), and a GAP-based heuristic procedure is defined for the problem. We define a two-phase heuristic for the FMGL problem and present computational experience with both heuristics. The FMRCP heuristic is shown to solve problems that exhibit a dependent-demand relation within the FMS and with FMS capacity utilization as high as 99 percent. The FMGL heuristic requires very little CPU time and obtains solutions to the test problems that are on average within 1.5 percent of a theoretical lower bound. This FMS/MRP production planning framework, together with the resulting models, constitutes an important step in the integration of FMS technology with MRP production planning. The hierarchical planning mechanism directly provides for system-level MRP planning priorities to induce appropriate production planning and control objectives on the FMS while simultaneously allowing for necessary feedback from the FMS. Moreover, by demonstrating the tractability of the FMRCP and FMGL problems, this research establishes the necessary groundwork upon which to explore systemwide issues pertaining to the coordination of the hierarchical structure.     

Short-term action of insulin on Aplysia neurons: Generation of a possible novel modulator of ion channels

In mollusks as in other animals, peptides can act as hormones, growth factors, and neurotransmitters. The presence of insulin in vertebrate brain as well as its actions on nerve cells led us to examine the electrophysiological effects of the mammalian hormone on Aplysia neurons. Application of insulin extracellularly causes hyperpolarization of L14 and L10, identified neurons of the abdominal ganglion. This hyperpolarization is associated with a decreased membrane conductance that reverses at ?35 mV. We also injected inositol phosphate glycan (IPG) into the identified neurons. This complex sugar, which was purified from rat liver and which is a putative second messenger for insulin in nonneural vertebrate cells (Saltiel and Cuatrecasas, 1986; Saltiel, Osterman, and Darnell, 1988), causes hyperpolarization with decreased membrane conductance in L14 and L10 similar to the effects of insulin. Furthermore, exposure of isolated ganglia to insulin results in the generation of IPG with a compensating decrease in its glycosyl-phosphatidylinositol precursor. We suggest that, in addition to its other roles, insulin may function as a neuropeptide transmitter using IPG as a second messenger.     

Pheromone-mediated sexual selection in the mothUtetheisa ornatrix: Olfactory receptor neurons responsive to a male-produced pheromone

Male Utetheisa ornatrixhave a pair of eversible glandular brushes (coremata) which are displayed during precopulatory interactions with the female. Earlier studies have shown that a pheromone associated with the coremata, hydroxydanaidal (HD), is derived by the males from pyrrolizidine alkaloids (PAs) that they sequester as larvae from their foodplants (Crotalariaspp.) The PAs impart a distastefulness upon Utetheisathat protects both larvae and adults against predation. The receptor neurons specialized for detection of HD are housed in sensilla whose morphological features, as revealed by scanning electron microscopy, classify them as sensilla basiconica. The sensitivity and dynamic range of these receptor neurons were largely unaffected by whether the females were raised on an alkaloid-free diet or on a diet supplemented with Crotalariaseeds. Acetylation of the hydroxyl group of HD substantially reduced the activity of the molecule. None of the antennal sensilla examined contained receptor neurons sensitive to a PA (monocrotaline) or its N-oxide.     

Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor

Conclusion Experimental evidence has accumulated over the past few years to suggest that the GPI protein anchor may play a broad role in the regulation of membrane protein function. The significant changes in the biophysical properties of proteins that are membrane-anchored through GPI in lieu of a hydrophobic transmembrane peptide indicates a variety phobic transmembrane peptide indicates a variety of potential new functions served by the anchor structure itself. Moreover, the number of structural variations within the family of GPI molecules indicates a further opportunity for subspecialization of such anchored proteins, especially regarding cellular localization, mobility, metabolism and susceptibility to enzymatically-induced release. It is likely that further exploration of the structure and function of the GPI anchor may reveal additional roles for this unusual mechanism of membrane-protein attachment.     

Electron spin resonance evidence for the formation of free radicals in plants exposed to ozone

Electron spin resonance (ESR) spectroscopy was used to demonstrate that free radicals are formed in O₃-fumigated plant leaves prior to the formation of visible leaf injury. ESR signals with a g-value of 2.0037 to 2.0043, were observed in pea ( Pisum sativum L. cv. Feltham first) and bean ( Phaseolus vulgaris L. cv. Pinto) plants that had been fumigated for 4 h with 70–300 nl l⁻¹ of ozone after they had been treated with the spin-trap N- t -butyl-α-phenylnitrone (PBN). The size of the ESR signals increased with the concentration of ozone used but the nature of the trapped radicals could not be identified. However, further experiments using an inhibitor of ethylene biosynthesis, arninoethoxyvinyl glycine (AVG), showed that the reaction between ozone and ethylene is the cause for ozone toxicity.     

The transport of class I major histocompatibility complex antigens is determined by sequences in the α1 and α2 protein domains

The transport of human-mouse hybrid class I histocompatibility antigens has been studied in a mutant human cell line, 174 × CEM.T2 (T2). T2, a somatic cell hybrid of human B- and T-lymphoblastoid cell lines (B-LCL and T-LCL, respectively), synthesizes HLA-A2 and HLA-B5 glycoproteins, but expresses only low levels of A2 and undetectable levels of B5 at the cell surface. We have previously shown that the products of human class I genes introduced into T2 by transfection behave like the endogenous HLA-B5 glycoproteins, while the products of mouse class I alleles similarly introduced are transported normally to the cell surface. We have now determined that the surface expression of class I glycoproteins in T2 depends on the origin of the ₁ and ₂ domains. Human (HLA-B7) and mouse (H-2D ^p ) hybrid class I genes, encoding the leader, ₁, and ₂ sequences of one species fused to the ₃, transmembrane, and cytoplasmic domains of the other, were transfected into T2. Normal surface expression of the hybrid class I molecule was observed in T2 only when the leader, ₁, and ₂-encoding exons were derived from the mouse gene. The reciprocal construct, encoding human leader, ₁, and ₂ domains fused to the mouse ₃, transmembrane, and cytoplasmic regions, resulted in biosynthesis of a hybrid glycoprotein which was not transported to the cell surface. The products of both constructs were expressed normally in control cells. The effects of glycosylation on class I antigen transport were also studied using mutant class I constructs with altered glycosylation sites. Two mutant B7 genes encoding either an extra glycosylation site at position 176 or no glycosylation sites were transfected into T2. These mutant products were expressed at the cell surface in control cells, but were synthesized and not surface-expressed in T2. These data demonstrate that the HLA/H-2 transport dichotomy in T2 is a function of the origin of the ₁ and/or ₂ domains of the class I glycoprotein, and is not a reflection of glycosylation differences between the human and mouse molecules. Offprint requests to: P. Cresswell.